SOD1

Superoxide dismutase sod1

Reviewed UniProt entries for SOD1 and its protein partners


UniProt code UniProt Name Protein Name Gene Name Organism Length
Q6T3B0 SODC_PAESI Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) SOD1 Paecilomyces sinensis 154
P13926 SOD1A_XENLA Superoxide dismutase [Cu-Zn] A (XSODA) (EC 1.15.1.1) sod1-a Xenopus laevis (African clawed frog) 151
P15107 SOD1B_XENLA Superoxide dismutase [Cu-Zn] B (XSODB) (EC 1.15.1.1) sod1-b Xenopus laevis (African clawed frog) 151
O42724 SODC1_DEBHA Superoxide dismutase [Cu-Zn] 1 (EC 1.15.1.1) SOD1 DEHA2G17732g Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii) 154
P93258 SODC1_MESCR Superoxide dismutase [Cu-Zn] 1 (EC 1.15.1.1) SODCC.1 SOD SOD1 Mesembryanthemum crystallinum (Common ice plant) (Cryophytum crystallinum) 152
Q9SQL5 SODC_ANACO Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) SOD1 Ananas comosus (Pineapple) (Ananas ananas) 152
Q751L8 SODC_ASHGO Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) SOD1 AGL321W Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii) 154
Q52RN5 SODC_BOSMU Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) SOD1 Bos mutus grunniens (Wild yak) (Bos grunniens) 152
Q70Q35 SODC_BOTFU Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) sod1 Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea) 154
P00442 SODC_BOVIN Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) SOD1 Bos taurus (Bovine) 152
A8XCP3 SODC_CAEBR Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) sod-1 CBG11197 Caenorhabditis briggsae 180
P34697 SODC_CAEEL Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) sod-1 C15F1.7 Caenorhabditis elegans 180
Q8HXP8 SODC_CALJA Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) SOD1 Callithrix jacchus (White-tufted-ear marmoset) 154
O59924 SODC_CANAX Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) SOD1 Candida albicans (Yeast) 154
Q8WNN6 SODC_CANFA Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) SOD1 Canis familiaris (Dog) (Canis lupus familiaris) 153
Q6FWL5 SODC_CANGA Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) SOD1 CAGL0C04741g Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) 154
Q5FB29 SODC_CAPHI Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) SOD1 Capra hircus (Goat) 152
P33431 SODC_CAVPO Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) SOD1 Cavia porcellus (Guinea pig) 153
Q8HXP9 SODC_CEBAP Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) SOD1 Cebus apella (Brown-capped capuchin) 154
O46412 SODC_CEREL Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) SOD1 Cervus elaphus (Red deer) 152
P80566 SODC_CHICK Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) SOD1 Gallus gallus (Chicken) 154
Q96VL0 SODC_CLAPU Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) SOD1 Claviceps purpurea (Ergot fungus) (Sphacelia purpurea) 154
O94178 SODC_COLGL Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) SOD1 Colletotrichum gloeosporioides (Anthracnose fungus) (Glomerella cingulata) 154
Q8J0N2 SODC_CORMI Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) SOD1 Cordyceps militaris (Caterpillar fungus) 154
Q9C0N4 SODC_CRYGA Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) SOD1 Cryptococcus gattii (Filobasidiella gattii) (Cryptococcus bacillisporus) 154
O73872 SODC_DANRE Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) sod1 cuzn Danio rerio (Zebrafish) (Brachydanio rerio) 154
P00443 SODC_HORSE Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) SOD1 Equus caballus (Horse) 154
Q8HXQ3 SODC_HYLLA Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) SOD1 Hylobates lar (Common gibbon) (White-handed gibbon) 154
Q6CPE2 SODC_KLULA Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) SOD1 KLLA0E05522g Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica) 155
P81036 SODC_LAMCR Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) (Fragment) sod1 Lampanyctus crocodilus (Jewel lanternfish) (Gasteropelecus crocodilus) 139
P23417 SODC_LITCT Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) (Fragment) sod1 Lithobates catesbeiana (American bullfrog) (Rana catesbeiana) 24
Q8HXQ1 SODC_MACFA Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) SOD1 QmoA-14762 Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey) 154
Q8HXQ2 SODC_MACFU Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) SOD1 Macaca fuscata fuscata (Japanese macaque) 154
Q8HXQ0 SODC_MACMU Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) SOD1 Macaca mulatta (Rhesus macaque) 154
P08228 SODC_MOUSE Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) Sod1 Mus musculus (Mouse) 154
P07509 SODC_NEUCR Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) sod-1 NCU02133 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) 154
P24706 SODC_ONCVO Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) sod-1 sod1 Onchocerca volvulus 158
Q8J0N3 SODC_PAETN Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) SOD1 Paecilomyces tenuipes 154
P60052 SODC_PANTR Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) SOD1 Pan troglodytes (Chimpanzee) 154
P83129 SODC_PAROL Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) (Fragment) sod1 Paralichthys olivaceus (Bastard halibut) (Hippoglossus olivaceus) 26
P04178 SODC_PIG Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) SOD1 Sus scrofa (Pig) 153
Q711T9 SODC_PODAS Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) SOD1 Podospora anserina (Pleurage anserina) 154
Q8HXQ4 SODC_PONPY Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) SOD1 Pongo pygmaeus (Bornean orangutan) 155
P11418 SODC_PRIGL Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) sod1 Prionace glauca (Blue shark) (Squalus glaucus) 152
P09212 SODC_RABIT Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) SOD1 Oryctolagus cuniculus (Rabbit) 153
P07632 SODC_RAT Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) Sod1 Rattus norvegicus (Rat) 154
P28758 SODC_SCHPO Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) sod1 SPAC821.10c Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) 154
P09670 SODC_SHEEP Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) SOD1 Ovis aries (Sheep) 152
Q7M1R5 SODC_SOYBN Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) SOD1 Glycine max (Soybean) (Glycine hispida) 152
Q0IIW3 SODC_XENTR Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) sod1 Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) 151
P03946 SODC_XIPGL Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) sod1 Xiphias gladius (Swordfish) (Tetrapterus imperator) 152
Q6C662 SODC_YARLI Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) SOD1 YALI0E12133g Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica) 154
P00445 SODC_YEAST Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) SOD1 YJR104C J1968 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Bakers yeast) 154
P00441 SODC_HUMAN Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) (Superoxide dismutase 1) (hSod1) SOD1 Homo sapiens (Human) 154

Small molecules tested in SOD1 binding assays:

32 datapoints for 20 distinct small molecules


Name Mppquinazoline
Affinity None
Assay description None
-- Direct single protein target assigned: SODC_HUMAN (Expert curation) --
DOI http://www.ncbi.nlm.nih.gov/pubmed/23278398
Doc title X-ray Crystallography and Computational Docking for the Detection and Development of Protein-Ligand Interactions
PDB 4A7G - (12I)

Name diazepanquinazoline
Affinity None
Assay description None
-- Direct single protein target assigned: SODC_HUMAN (Expert curation) --
DOI http://www.ncbi.nlm.nih.gov/pubmed/23278398
Doc title X-ray Crystallography and Computational Docking for the Detection and Development of Protein-Ligand Interactions
PDB 4A7Q - (4MQ)

Name CHEMBL1091583
Affinity Not Active
Assay description Binding affinity to human GST-SOD1 expressed in Escherichia coli Rosetta at 100 uM in presence of human plasma by reverse phase HPLC analysis
-- Direct single protein target assigned: SODC_HUMAN (Autocuration) --
DOI http://www.ncbi.nlm.nih.gov/pubmed/20232802
Doc title Improving binding specificity of pharmacological chaperones that target mutant superoxide dismutase-1 linked to familial amyotrophic lateral sclerosis using computational methods.
PDB None

Name CHEMBL1091584
Affinity Not Active
Assay description Binding affinity to human GST-SOD1 expressed in Escherichia coli Rosetta at 100 uM in presence of human plasma by reverse phase HPLC analysis
-- Direct single protein target assigned: SODC_HUMAN (Autocuration) --
DOI http://www.ncbi.nlm.nih.gov/pubmed/20232802
Doc title Improving binding specificity of pharmacological chaperones that target mutant superoxide dismutase-1 linked to familial amyotrophic lateral sclerosis using computational methods.
PDB None

Name CHEMBL1092384
Affinity Not Active
Assay description Binding affinity to human GST-SOD1 expressed in Escherichia coli Rosetta at 100 uM in presence of human plasma by reverse phase HPLC analysis
-- Direct single protein target assigned: SODC_HUMAN (Autocuration) --
DOI http://www.ncbi.nlm.nih.gov/pubmed/20232802
Doc title Improving binding specificity of pharmacological chaperones that target mutant superoxide dismutase-1 linked to familial amyotrophic lateral sclerosis using computational methods.
PDB None

Name CHEMBL1092602
Affinity Not Active
Assay description Binding affinity to human GST-SOD1 expressed in Escherichia coli Rosetta at 100 uM in presence of human plasma by reverse phase HPLC analysis
-- Direct single protein target assigned: SODC_HUMAN (Autocuration) --
DOI http://www.ncbi.nlm.nih.gov/pubmed/20232802
Doc title Improving binding specificity of pharmacological chaperones that target mutant superoxide dismutase-1 linked to familial amyotrophic lateral sclerosis using computational methods.
PDB None

Name CHEMBL1092603
Affinity Not Active
Assay description Binding affinity to human GST-SOD1 expressed in Escherichia coli Rosetta at 100 uM in presence of human plasma by reverse phase HPLC analysis
-- Direct single protein target assigned: SODC_HUMAN (Autocuration) --
DOI http://www.ncbi.nlm.nih.gov/pubmed/20232802
Doc title Improving binding specificity of pharmacological chaperones that target mutant superoxide dismutase-1 linked to familial amyotrophic lateral sclerosis using computational methods.
PDB None

Name CHEMBL1092604
Affinity Not Active
Assay description Binding affinity to human GST-SOD1 expressed in Escherichia coli Rosetta at 100 uM in presence of human plasma by reverse phase HPLC analysis
-- Direct single protein target assigned: SODC_HUMAN (Autocuration) --
DOI http://www.ncbi.nlm.nih.gov/pubmed/20232802
Doc title Improving binding specificity of pharmacological chaperones that target mutant superoxide dismutase-1 linked to familial amyotrophic lateral sclerosis using computational methods.
PDB None

Name CHEMBL124937
Affinity Not Active
Assay description Binding affinity to human GST-SOD1 expressed in Escherichia coli Rosetta at 100 uM in presence of human plasma by reverse phase HPLC analysis
-- Direct single protein target assigned: SODC_HUMAN (Autocuration) --
DOI http://www.ncbi.nlm.nih.gov/pubmed/20232802
Doc title Improving binding specificity of pharmacological chaperones that target mutant superoxide dismutase-1 linked to familial amyotrophic lateral sclerosis using computational methods.
PDB None

Name CHEMBL1672028
Affinity IC50 = 96.6uM
Assay description Inhibition of human Cu-Zn superoxide dismutase assessed as inhibition of NADPH reduction
-- Direct single protein target assigned: SODC_HUMAN (Autocuration) --
DOI http://www.ncbi.nlm.nih.gov/pubmed/21229977
Doc title In vivo trypanosomicidal activity of imidazole- or pyrazole-based benzo[g]phthalazine derivatives against acute and chronic phases of Chagas disease.
PDB None

Name CHEMBL1672029
Affinity IC50 = 103.3uM
Assay description Inhibition of human Cu-Zn superoxide dismutase assessed as inhibition of NADPH reduction
-- Direct single protein target assigned: SODC_HUMAN (Autocuration) --
DOI http://www.ncbi.nlm.nih.gov/pubmed/21229977
Doc title In vivo trypanosomicidal activity of imidazole- or pyrazole-based benzo[g]phthalazine derivatives against acute and chronic phases of Chagas disease.
PDB None

Name CHEMBL2179265
Affinity IC50 = 65.98uM
Assay description Inhibition of SOD1 in human erythrocytes by spectrophotometry
-- Direct single protein target assigned: SODC_HUMAN (Autocuration) --
DOI http://www.ncbi.nlm.nih.gov/pubmed/23043291
Doc title Phthalazine derivatives containing imidazole rings behave as Fe-SOD inhibitors and show remarkable anti-T. cruzi activity in immunodeficient-mouse mode of infection.
PDB None

Name CHEMBL2179266
Affinity IC50 = 83.12uM
Assay description Inhibition of SOD1 in human erythrocytes by spectrophotometry
-- Direct single protein target assigned: SODC_HUMAN (Autocuration) --
DOI http://www.ncbi.nlm.nih.gov/pubmed/23043291
Doc title Phthalazine derivatives containing imidazole rings behave as Fe-SOD inhibitors and show remarkable anti-T. cruzi activity in immunodeficient-mouse mode of infection.
PDB None

Name CHEMBL2179267
Affinity IC50 = 125.32uM
Assay description Inhibition of SOD1 in human erythrocytes by spectrophotometry
-- Direct single protein target assigned: SODC_HUMAN (Autocuration) --
DOI http://www.ncbi.nlm.nih.gov/pubmed/23043291
Doc title Phthalazine derivatives containing imidazole rings behave as Fe-SOD inhibitors and show remarkable anti-T. cruzi activity in immunodeficient-mouse mode of infection.
PDB None

Name CHEMBL2179268
Affinity IC50 = 71.46uM
Assay description Inhibition of SOD1 in human erythrocytes by spectrophotometry
-- Direct single protein target assigned: SODC_HUMAN (Autocuration) --
DOI http://www.ncbi.nlm.nih.gov/pubmed/23043291
Doc title Phthalazine derivatives containing imidazole rings behave as Fe-SOD inhibitors and show remarkable anti-T. cruzi activity in immunodeficient-mouse mode of infection.
PDB None

Name CHEMBL259219
Affinity Active
Assay description Stimulation of SOD activity in Nicotiana tabacum after 3 days
-- Homologous single protein target assigned: SODC_HUMAN (Autocuration) --
DOI http://www.ncbi.nlm.nih.gov/pubmed/18178446
Doc title Synthesis and antiviral activities of novel chiral cyanoacrylate derivatives with (E) configuration.
PDB None

Name CHEMBL272641
Affinity Inhibition = 18%
Assay description inhibition of CuZn-SOD in human erythrocytes at 125 uM
-- Direct single protein target assigned: SODC_HUMAN (Autocuration) --
DOI http://www.ncbi.nlm.nih.gov/pubmed/18293910
Doc title Efficient inhibition of iron superoxide dismutase and of Trypanosoma cruzi growth by benzo[g]phthalazine derivatives functionalized with one or two imidazole rings.
PDB None

Name CHEMBL272641
Affinity Inhibition = 2%
Assay description inhibition of CuZn-SOD in human erythrocytes at 2.5 uM
-- Direct single protein target assigned: SODC_HUMAN (Autocuration) --
DOI http://www.ncbi.nlm.nih.gov/pubmed/18293910
Doc title Efficient inhibition of iron superoxide dismutase and of Trypanosoma cruzi growth by benzo[g]phthalazine derivatives functionalized with one or two imidazole rings.
PDB None

Name CHEMBL272641
Affinity IC50 = 67.9uM
Assay description Inhibition of human Cu-Zn superoxide dismutase assessed as inhibition of NADPH reduction
-- Direct single protein target assigned: SODC_HUMAN (Autocuration) --
DOI http://www.ncbi.nlm.nih.gov/pubmed/21229977
Doc title In vivo trypanosomicidal activity of imidazole- or pyrazole-based benzo[g]phthalazine derivatives against acute and chronic phases of Chagas disease.
PDB None

Name CHEMBL272641
Affinity Inhibition = 12%
Assay description inhibition of CuZn-SOD in human erythrocytes at 25 uM
-- Direct single protein target assigned: SODC_HUMAN (Autocuration) --
DOI http://www.ncbi.nlm.nih.gov/pubmed/18293910
Doc title Efficient inhibition of iron superoxide dismutase and of Trypanosoma cruzi growth by benzo[g]phthalazine derivatives functionalized with one or two imidazole rings.
PDB None

Name CHEMBL272808
Affinity Inhibition = 0%
Assay description inhibition of CuZn-SOD in human erythrocytes at 25 uM
-- Direct single protein target assigned: SODC_HUMAN (Autocuration) --
DOI http://www.ncbi.nlm.nih.gov/pubmed/18293910
Doc title Efficient inhibition of iron superoxide dismutase and of Trypanosoma cruzi growth by benzo[g]phthalazine derivatives functionalized with one or two imidazole rings.
PDB None

Name CHEMBL272808
Affinity IC50 = 786.9uM
Assay description Inhibition of human Cu-Zn superoxide dismutase assessed as inhibition of NADPH reduction
-- Direct single protein target assigned: SODC_HUMAN (Autocuration) --
DOI http://www.ncbi.nlm.nih.gov/pubmed/21229977
Doc title In vivo trypanosomicidal activity of imidazole- or pyrazole-based benzo[g]phthalazine derivatives against acute and chronic phases of Chagas disease.
PDB None

Name CHEMBL272808
Affinity Inhibition = 0%
Assay description inhibition of CuZn-SOD in human erythrocytes at 2.5 uM
-- Direct single protein target assigned: SODC_HUMAN (Autocuration) --
DOI http://www.ncbi.nlm.nih.gov/pubmed/18293910
Doc title Efficient inhibition of iron superoxide dismutase and of Trypanosoma cruzi growth by benzo[g]phthalazine derivatives functionalized with one or two imidazole rings.
PDB None

Name CHEMBL272808
Affinity Inhibition = 11%
Assay description inhibition of CuZn-SOD in human erythrocytes at 125 uM
-- Direct single protein target assigned: SODC_HUMAN (Autocuration) --
DOI http://www.ncbi.nlm.nih.gov/pubmed/18293910
Doc title Efficient inhibition of iron superoxide dismutase and of Trypanosoma cruzi growth by benzo[g]phthalazine derivatives functionalized with one or two imidazole rings.
PDB None

Name CHEMBL273030
Affinity Inhibition = 5%
Assay description inhibition of CuZn-SOD in human erythrocytes at 25 uM
-- Direct single protein target assigned: SODC_HUMAN (Autocuration) --
DOI http://www.ncbi.nlm.nih.gov/pubmed/18293910
Doc title Efficient inhibition of iron superoxide dismutase and of Trypanosoma cruzi growth by benzo[g]phthalazine derivatives functionalized with one or two imidazole rings.
PDB None

Name CHEMBL273030
Affinity Inhibition = 0%
Assay description inhibition of CuZn-SOD in human erythrocytes at 2.5 uM
-- Direct single protein target assigned: SODC_HUMAN (Autocuration) --
DOI http://www.ncbi.nlm.nih.gov/pubmed/18293910
Doc title Efficient inhibition of iron superoxide dismutase and of Trypanosoma cruzi growth by benzo[g]phthalazine derivatives functionalized with one or two imidazole rings.
PDB None

Name CHEMBL273030
Affinity Inhibition = 6%
Assay description inhibition of CuZn-SOD in human erythrocytes at 125 uM
-- Direct single protein target assigned: SODC_HUMAN (Autocuration) --
DOI http://www.ncbi.nlm.nih.gov/pubmed/18293910
Doc title Efficient inhibition of iron superoxide dismutase and of Trypanosoma cruzi growth by benzo[g]phthalazine derivatives functionalized with one or two imidazole rings.
PDB None

Name CHEMBL273030
Affinity IC50 = 365.8uM
Assay description Inhibition of human Cu-Zn superoxide dismutase assessed as inhibition of NADPH reduction
-- Direct single protein target assigned: SODC_HUMAN (Autocuration) --
DOI http://www.ncbi.nlm.nih.gov/pubmed/21229977
Doc title In vivo trypanosomicidal activity of imidazole- or pyrazole-based benzo[g]phthalazine derivatives against acute and chronic phases of Chagas disease.
PDB None

Name CHEMBL405899
Affinity Inhibition = 22%
Assay description inhibition of CuZn-SOD in human erythrocytes at 25 uM
-- Direct single protein target assigned: SODC_HUMAN (Autocuration) --
DOI http://www.ncbi.nlm.nih.gov/pubmed/18293910
Doc title Efficient inhibition of iron superoxide dismutase and of Trypanosoma cruzi growth by benzo[g]phthalazine derivatives functionalized with one or two imidazole rings.
PDB None

Name CHEMBL405899
Affinity Inhibition = 7%
Assay description inhibition of CuZn-SOD in human erythrocytes at 2.5 uM
-- Direct single protein target assigned: SODC_HUMAN (Autocuration) --
DOI http://www.ncbi.nlm.nih.gov/pubmed/18293910
Doc title Efficient inhibition of iron superoxide dismutase and of Trypanosoma cruzi growth by benzo[g]phthalazine derivatives functionalized with one or two imidazole rings.
PDB None

Name CHEMBL405899
Affinity IC50 = 129.3uM
Assay description Inhibition of human Cu-Zn superoxide dismutase assessed as inhibition of NADPH reduction
-- Direct single protein target assigned: SODC_HUMAN (Autocuration) --
DOI http://www.ncbi.nlm.nih.gov/pubmed/21229977
Doc title In vivo trypanosomicidal activity of imidazole- or pyrazole-based benzo[g]phthalazine derivatives against acute and chronic phases of Chagas disease.
PDB None

Name CHEMBL405899
Affinity Inhibition = 27%
Assay description inhibition of CuZn-SOD in human erythrocytes at 125 uM
-- Direct single protein target assigned: SODC_HUMAN (Autocuration) --
DOI http://www.ncbi.nlm.nih.gov/pubmed/18293910
Doc title Efficient inhibition of iron superoxide dismutase and of Trypanosoma cruzi growth by benzo[g]phthalazine derivatives functionalized with one or two imidazole rings.
PDB None

109 PDB entries for SOD1 and its protein partners


1AZV
Subunit asymmetry in the three-dimensional structure of a human CuZnSOD mutant found in familial amyotrophic lateral sclerosis.

Entity type Code Description
polypeptide(L) P00441 COPPER/ZINC SUPEROXIDE DISMUTASE
Ligand CU COPPER (II) ION

1B4L
A structure-based mechanism for copper-zinc superoxide dismutase.

Entity type Code Description
polypeptide(L) P00445 PROTEIN (CU/ZN SUPEROXIDE DISMUTASE)
Ligand CU COPPER (II) ION

1B4T
A structure-based mechanism for copper-zinc superoxide dismutase.

Entity type Code Description
polypeptide(L) P00445 PROTEIN (CU/ZN SUPEROXIDE DISMUTASE)
Ligand CU COPPER (II) ION

1BA9
Solution structure of reduced monomeric Q133M2 copper, zinc superoxide dismutase (SOD). Why is SOD a dimeric enzyme?.

Entity type Code Description
polypeptide(L) P00441 SUPEROXIDE DISMUTASE
Ligand CU1 COPPER (I) ION

1CB4
Crystallographic structures of bovine copper-zinc superoxide dismutase reveal asymmetry in two subunits: functionally important three and five coordinate copper sites captured in the same crystal.

Entity type Code Description
polypeptide(L) P00442 PROTEIN (SUPEROXIDE DISMUTASE)
Ligand CU COPPER (II) ION

1CBJ
Crystallographic structures of bovine copper-zinc superoxide dismutase reveal asymmetry in two subunits: functionally important three and five coordinate copper sites captured in the same crystal.

Entity type Code Description
polypeptide(L) P00442 PROTEIN (SUPEROXIDE DISMUTASE)
Ligand CU COPPER (II) ION

1COB
Crystal structure solution and refinement of the semisynthetic cobalt-substituted bovine erythrocyte superoxide dismutase at 2.0 A resolution.

Entity type Code Description
polypeptide(L) P00442 SUPEROXIDE DISMUTASE
Ligand CU COPPER (II) ION

1DSW
The solution structure of a monomeric, reduced form of human copper,zinc superoxide dismutase bearing the same charge as the native protein.

Entity type Code Description
polypeptide(L) P00441 SUPEROXIDE DISMUTASE (CU-ZN)
Ligand CU COPPER (II) ION

1E9O
Conformational Variability of the Cu Site in One Subunit of Bovine Cuzn Superoxide Dismutase: The Importance of Mobility in the Glu119-Leu142 Loop Region for Catalytic Function

Entity type Code Description
polypeptide(L) 1E9O SUPEROXIDE DISMUTASE
polypeptide(L) P00442 SUPEROXIDE DISMUTASE
polypeptide(L) 1E9O SUPEROXIDE DISMUTASE
polypeptide(L) P00442 SUPEROXIDE DISMUTASE
Ligand CU COPPER (II) ION

1E9P
Conformational Variability of the Cu Site in One Subunit of Bovine Cuzn Superoxide Dismutase: The Importance of Mobility in the Glu119-Leu142 Loop Region for Catalytic Function.

Entity type Code Description
polypeptide(L) P00442 SUPEROXIDE DISMUTASE
polypeptide(L) P00442 SUPEROXIDE DISMUTASE
Ligand CU COPPER (II) ION

1E9Q
Conformational Variability of the Cu Site in One Subunit of Bovine Cuzn Superoxide Dismutase: The Importance of Mobility in the Glu119-Leu142 Loop Region for Catalytic Function

Entity type Code Description
polypeptide(L) P00442 SUPEROXIDE DISMUTASE
polypeptide(L) P00442 SUPEROXIDE DISMUTASE
Ligand CU COPPER (II) ION

1FUN
Computational, pulse-radiolytic, and structural investigations of lysine-136 and its role in the electrostatic triad of human Cu,Zn superoxide dismutase.

Entity type Code Description
polypeptide(L) P00441 SUPEROXIDE DISMUTASE
Ligand CU COPPER (II) ION

1HL4
The Structure of Holo and Metal-Deficient Wild-Type Human Cu, Zn Superoxide Dismutase and its Relevance to Familial Amyotrophic Lateral Sclerosis

Entity type Code Description
polypeptide(L) 1HL4 SUPEROXIDE DISMUTASE
polypeptide(L) P00441 SUPEROXIDE DISMUTASE

1HL5
The Structure of Holo and Metal-Deficient Wild-Type Human Cu, Zn Superoxide Dismutase and its Relevance to Familial Amyotrophic Lateral Sclerosis

Entity type Code Description
polypeptide(L) P00441 SUPEROXIDE DISMUTASE
Ligand CU COPPER (II) ION

1JCV
Unusual trigonal-planar copper configuration revealed in the atomic structure of yeast copper-zinc superoxide dismutase.

Entity type Code Description
polypeptide(L) P00445 CU/ZN SUPEROXIDE DISMUTASE
Ligand CU COPPER (II) ION

1JK9
Heterodimeric structure of superoxide dismutase in complex with its metallochaperone.

Entity type Code Description
polypeptide(L) P00445 superoxide dismutase
polypeptide(L) P40202 copper chaperone for superoxide dismutase

1KMG
Structure and dynamics of copper-free SOD: The protein before binding copper.

Entity type Code Description
polypeptide(L) P00441 Superoxide Dismutase

1L3N
The solution structure of reduced dimeric copper zinc superoxide dismutase. The structural effects of dimerization

Entity type Code Description
polypeptide(L) P00441 superoxide dismutase [Cu-Zn]
Ligand CU1 COPPER (I) ION

1MFM
The crystal structure of the monomeric human SOD mutant F50E/G51E/E133Q at atomic resolution. The enzyme mechanism revisited.

Entity type Code Description
polypeptide(L) P00441 PROTEIN (COPPER,ZINC SUPEROXIDE DISMUTASE)
Ligand CU COPPER (II) ION

1N18
Insights into Lou Gehrig's disease from the structure and instability of the A4V mutant of human Cu,Zn superoxide dismutase.

Entity type Code Description
polypeptide(L) P00441 Superoxide dismutase [Cu-Zn]
Ligand CU1 COPPER (I) ION

1N19
Insights into Lou Gehrig's disease from the structure and instability of the A4V mutant of human Cu,Zn superoxide dismutase.

Entity type Code Description
polypeptide(L) P00441 Superoxide Dismutase [Cu-Zn]
Ligand CU1 COPPER (I) ION

1OEZ
Amyloid-Like Filaments and Water-Filled Nanotubes Formed by Sod1 Mutant Proteins Linked to Familial Als

Entity type Code Description
polypeptide(L) P00441 SUPEROXIDE DISMUTASE [CU-ZN]

1OZT
Amyloid-like Filaments and Water-filled Nanotubes Formed by SOD1 Mutant Proteins Linked to Familial ALS

Entity type Code Description
polypeptide(L) P00441 Superoxide dismutase [Cu-Zn]

1OZU
Amyloid-like Filaments and Water-filled Nanotubes Formed by SOD1 Mutant Proteins Linked to Familial ALS

Entity type Code Description
polypeptide(L) P00441 Superoxide dismutase [Cu-Zn]

1P1V
An Alternative Mechanism of Bicarbonate-mediated Peroxidation by Copper-Zinc Superoxide Dismutase: RATES ENHANCED VIA PROPOSED ENZYME-ASSOCIATED PEROXYCARBONATE INTERMEDIATE

Entity type Code Description
polypeptide(L) P00441 Superoxide dismutase [Cu-Zn]

1PTZ
ALS Mutants of Human Superoxide Dismutase Form Fibrous Aggregates Via Framework Destabilization

Entity type Code Description
polypeptide(L) P00441 Superoxide dismutase [Cu-Zn]
Ligand CU1 COPPER (I) ION

1PU0
ALS Mutants of Human Superoxide Dismutase Form Fibrous Aggregates Via Framework Destabilization

Entity type Code Description
polypeptide(L) P00441 Superoxide dismutase [Cu-Zn]
Ligand CU1 COPPER (I) ION

1Q0E
Structure of fully reduced bovine copper zinc superoxide dismutase at 1.15 A.

Entity type Code Description
polypeptide(L) P00442 Superoxide dismutase [Cu-Zn]
Ligand CU COPPER (II) ION

1RK7
Solution structure of Apo Cu,Zn Superoxide Dismutase: Role of Metal Ions in Protein Folding

Entity type Code Description
polypeptide(L) P00441 Superoxide dismutase [Cu-Zn]

1SDA
Crystal structure of peroxynitrite-modified bovine Cu,Zn superoxide dismutase.

Entity type Code Description
polypeptide(L) P00442 COPPER,ZINC SUPEROXIDE DISMUTASE
Ligand CU COPPER (II) ION

1SDY
Structure solution and molecular dynamics refinement of the yeast Cu,Zn enzyme superoxide dismutase.

Entity type Code Description
polypeptide(L) P00445 COPPER,ZINC SUPEROXIDE DISMUTASE
Ligand CU COPPER (II) ION

1SOS
Atomic structures of wild-type and thermostable mutant recombinant human Cu,Zn superoxide dismutase.

Entity type Code Description
polypeptide(L) P00441 SUPEROXIDE DISMUTASE
Ligand CU COPPER (II) ION

1SPD
Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxide dismutase.

Entity type Code Description
polypeptide(L) P00441 SUPEROXIDE DISMUTASE
Ligand CU COPPER (II) ION

1SXA
Crystal structure of reduced bovine erythrocyte superoxide dismutase at 1.9 A resolution.

Entity type Code Description
polypeptide(L) P00442 SUPEROXIDE DISMUTASE
Ligand CU COPPER (II) ION

1SXB
Crystal structure of reduced bovine erythrocyte superoxide dismutase at 1.9 A resolution.

Entity type Code Description
polypeptide(L) P00442 SUPEROXIDE DISMUTASE
Ligand CU COPPER (II) ION

1SXC
Crystal structure of reduced bovine erythrocyte superoxide dismutase at 1.9 A resolution.

Entity type Code Description
polypeptide(L) P00442 SUPEROXIDE DISMUTASE
Ligand CU COPPER (II) ION

1SXN
Crystallographic determination of reduced bovine superoxide dismutase at pH 5.0 and of anion binding to its active site.

Entity type Code Description
polypeptide(L) P00442 CU, ZN SUPEROXIDE DISMUTASE
Ligand CU COPPER (II) ION

1SXS
Crystallographic determination of reduced bovine superoxide dismutase at pH 5.0 and of anion binding to its active site

Entity type Code Description
polypeptide(L) P00442 PROTEIN (CU-ZN SUPEROXIDE DISMUTASE)
Ligand SCN THIOCYANATE ION
Ligand CU COPPER (II) ION

1SXZ
Crystallographic determination of reduced bovine superoxide dismutase at pH 5.0 and of anion binding to its active site

Entity type Code Description
polypeptide(L) P00442 PROTEIN (CU-ZN SUPEROXIDE DISMUTASE)
Ligand CU COPPER (II) ION
Ligand AZI AZIDE ION

1UXL
Dimer Destabilization in Superoxide Dismutase May Result in Disease-Causing Properties: Structures of Motor Neuron Disease Mutants

Entity type Code Description
polypeptide(L) P00441 SUPEROXIDE DISMUTASE [CU-ZN]
Ligand CU COPPER (II) ION

1UXM
Dimer Destabilization in Superoxide Dismutase May Result in Disease-Causing Properties: Structures of Motor Neuron Disease Mutants

Entity type Code Description
polypeptide(L) P00441 SUPEROXIDE DISMUTASE [CU-ZN]
Ligand CU COPPER (II) ION

1XSO
Three-dimensional structure of Xenopus laevis Cu,Zn superoxide dismutase b determined by X-ray crystallography at 1.5 A resolution.

Entity type Code Description
polypeptide(L) P15107 COPPER,ZINC SUPEROXIDE DISMUTASE
Ligand CU COPPER (II) ION

1YAZ
A structure-based mechanism for copper-zinc superoxide dismutase.

Entity type Code Description
polypeptide(L) P00445 PROTEIN (CU/ZN SUPEROXIDE DISMUTASE)
Ligand CU COPPER (II) ION
Ligand AZI AZIDE ION

1YSO
Unusual trigonal-planar copper configuration revealed in the atomic structure of yeast copper-zinc superoxide dismutase.

Entity type Code Description
polypeptide(L) P00445 YEAST CU, ZN SUPEROXIDE DISMUTASE
Ligand CU1 COPPER (I) ION

2AEO
Structural investigation of cisplatin-protein interactions: selective platination of His19 in a cuprozinc superoxide dismutase

Entity type Code Description
polypeptide(L) P00442 Superoxide dismutase [Cu-Zn]
Ligand CU COPPER (II) ION
Ligand NCP CIS-DIAMINODICHLOROPLATINUM

2AF2
Human SOD1 before harboring the catalytic metal: solution structure of copper-depleted, disulfide-reduced form

Entity type Code Description
polypeptide(L) P00441 Superoxide dismutase [Cu-Zn]

2C9S
Variable Metallation of Human Superoxide Dismutase: Atomic Resolution Crystal Structures of Cu-Zn, Zn-Zn and as-Isolated Wild-Type Enzymes.

Entity type Code Description
polypeptide(L) P00441 SUPEROXIDE DISMUTASE [CU-ZN]

2C9U
Variable Metallation of Human Superoxide Dismutase: Atomic Resolution Crystal Structures of Cu-Zn, Zn-Zn and as-Isolated Wild-Type Enzymes.

Entity type Code Description
polypeptide(L) P00441 SUPEROXIDE DISMUTASE [CU-ZN]
Ligand CU COPPER (II) ION

2C9V
Variable Metallation of Human Superoxide Dismutase: Atomic Resolution Crystal Structures of Cu-Zn, Zn-Zn and as-Isolated Wild-Type Enzymes.

Entity type Code Description
polypeptide(L) P00441 SUPEROXIDE DISMUTASE [CU-ZN]
Ligand CU COPPER (II) ION

2GBT
The Coupling between Disulphide Status, Metallation and Dimer Interface Strength in Cu/Zn Superoxide Dismutase

Entity type Code Description
polypeptide(L) P00441 Superoxide dismutase [Cu-Zn]
Ligand CU1 COPPER (I) ION

2GBU
The Coupling between Disulphide Status, Metallation and Dimer Interface Strength in Cu/Zn Superoxide Dismutase

Entity type Code Description
polypeptide(L) P00441 Superoxide dismutase [Cu-Zn]

2GBV
The Coupling between Disulphide Status, Metallation and Dimer Interface Strength in Cu/Zn Superoxide Dismutase

Entity type Code Description
polypeptide(L) P00441 Superoxide dismutase [Cu-Zn]
Ligand CU1 COPPER (I) ION

2JCW
A structure-based mechanism for copper-zinc superoxide dismutase.

Entity type Code Description
polypeptide(L) P00445 CU/ZN SUPEROXIDE DISMUTASE
Ligand CU1 COPPER (I) ION

2LU5
Structure and backbone dynamics of a microcrystalline metalloprotein by solid-state NMR.

Entity type Code Description
polypeptide(L) P00441 Superoxide dismutase [Cu-Zn]
Ligand CU COPPER (II) ION

2NNX
Disease-associated mutations at copper ligand histidine residues of superoxide dismutase 1 diminish the binding of copper and compromise dimer stability

Entity type Code Description
polypeptide(L) P00441 SUPEROXIDE DISMUTASE [CU-ZN]

2R27
Structural characterization of zinc-deficient human superoxide dismutase and implications for ALS.

Entity type Code Description
polypeptide(L) P00441 Superoxide dismutase [Cu-Zn]
Ligand CU COPPER (II) ION

2SOD
Determination and analysis of the 2 A-structure of copper, zinc superoxide dismutase.

Entity type Code Description
polypeptide(L) P00442 COPPER,ZINC SUPEROXIDE DISMUTASE
Ligand CU COPPER (II) ION

2V0A
Molecular Dynamics Using Atomic-Resolution Structure Reveal Structural Fluctuations that May Lead to Polymerization of Human Cu-Zn Superoxide Dismutase.

Entity type Code Description
polypeptide(L) P00441 SUPEROXIDE DISMUTASE
Ligand CU COPPER (II) ION

2VR6
Structures of the G85R Variant of Sod1 in Familial Amyotrophic Lateral Sclerosis.

Entity type Code Description
polypeptide(L) P00441 SUPEROXIDE DISMUTASE [CU-ZN]
Ligand CU COPPER (II) ION
Ligand SCN THIOCYANATE ION

2VR7
Structures of the G85R Variant of Sod1 in Familial Amyotrophic Lateral Sclerosis.

Entity type Code Description
polypeptide(L) 2VR7 SUPEROXIDE DISMUTASE [CU-ZN]
polypeptide(L) P00441 SUPEROXIDE DISMUTASE [CU-ZN]
Ligand CU COPPER (II) ION
Ligand SCN THIOCYANATE ION

2VR8
Structures of the G85R Variant of Sod1 in Familial Amyotrophic Lateral Sclerosis.

Entity type Code Description
polypeptide(L) 2VR8 SUPEROXIDE DISMUTASE [CU-ZN]
polypeptide(L) P00441 SUPEROXIDE DISMUTASE [CU-ZN]
Ligand CU COPPER (II) ION
Ligand SCN THIOCYANATE ION

2WKO
Structural and Biophysical Properties of Metal-Free Pathogenic Sod1 Mutants A4V and G93A.

Entity type Code Description
polypeptide(L) 2WKO SUPEROXIDE DISMUTASE [CU-ZN]
polypeptide(L) P00441 SUPEROXIDE DISMUTASE [CU-ZN]
polypeptide(L) 2WKO SUPEROXIDE DISMUTASE [CU-ZN]
polypeptide(L) P00441 SUPEROXIDE DISMUTASE [CU-ZN]
Ligand CU COPPER (II) ION

2WYT
Structural Discovery of Small Molecule Binding Sites in Cu-Zn Human Superoxide Dismutase Familial Amyotrophic Lateral Sclerosis Mutants Provides Insights for Lead Optimization.

Entity type Code Description
polypeptide(L) P00441 SUPEROXIDE DISMUTASE [CU-ZN]
Ligand CU COPPER (II) ION

2WYZ
Structural Discovery of Small Molecule Binding Sites in Cu-Zn Human Superoxide Dismutase Familial Amyotrophic Lateral Sclerosis Mutants Provides Insights for Lead Optimization.

Entity type Code Description
polypeptide(L) P00441 SUPEROXIDE DISMUTASE [CU-ZN]
Ligand CU COPPER (II) ION
Ligand U5P URIDINE-5'-MONOPHOSPHATE

2WZ0
Structural Discovery of Small Molecule Binding Sites in Cu-Zn Human Superoxide Dismutase Familial Amyotrophic Lateral Sclerosis Mutants Provides Insights for Lead Optimization.

Entity type Code Description
polypeptide(L) P00441 SUPEROXIDE DISMUTASE [CU-ZN]
Ligand CU COPPER (II) ION
Ligand ZZT 2-METHOXY-5-METHYLANILINE
Ligand DSN D-SERINE

2WZ5
Structural Discovery of Small Molecule Binding Sites in Cu-Zn Human Superoxide Dismutase Familial Amyotrophic Lateral Sclerosis Mutants Provides Insights for Lead Optimization.

Entity type Code Description
polypeptide(L) P00441 SUPEROXIDE DISMUTASE [CU-ZN]
Ligand CU COPPER (II) ION
Ligand MET METHIONINE

2WZ6
Structural Discovery of Small Molecule Binding Sites in Cu-Zn Human Superoxide Dismutase Familial Amyotrophic Lateral Sclerosis Mutants Provides Insights for Lead Optimization.

Entity type Code Description
polypeptide(L) P00441 SUPEROXIDE DISMUTASE [CU-ZN]
Ligand CU COPPER (II) ION
Ligand ZO0 4-(4-METHYL-1,4-DIAZEPAN-1-YL)-2-(TRIFLUOROMETHYL)QUINAZOLINE

2XJK
Folding Catalysis by Transient Coordination of Zn2+ to the Cu Ligands of the Als-Associated Enzyme Cu/Zn Superoxide Dismutase 1.

Entity type Code Description
polypeptide(L) P00441 SUPEROXIDE DISMUTASE [CU-ZN]
Ligand CU COPPER (II) ION

2XJL
Folding Catalysis by Transient Coordination of Zn2+ to the Cu Ligands of the Als-Associated Enzyme Cu/Zn Superoxide Dismutase 1.

Entity type Code Description
polypeptide(L) P00441 SUPEROXIDE DISMUTASE [CU-ZN]
Ligand PEG DI(HYDROXYETHYL)ETHER

2Z7U
Crystal structures of H2O2-treated Cu,Zn-superoxide dismutase

Entity type Code Description
polypeptide(L) P00442 Superoxide dismutase [Cu-Zn]
Ligand CU COPPER (II) ION

2Z7W
Crystal structures of H2O2-treated Cu,Zn-superoxide dismutase

Entity type Code Description
polypeptide(L) P00442 Superoxide dismutase [Cu-Zn]
Ligand CU COPPER (II) ION

2Z7Y
Crystal structure of H2O2-treated Cu,Zn-superoxide dismutase

Entity type Code Description
polypeptide(L) P00442 Superoxide dismutase [Cu-Zn]
Ligand CU COPPER (II) ION

2Z7Z
Crystal structure of H2O2-treated Cu,Zn-superoxide dismutase

Entity type Code Description
polypeptide(L) P00442 Superoxide dismutase [Cu-Zn]
Ligand CU COPPER (II) ION