21EN
Cryo-EM structure of monomeric Cu/Zn-superoxide dismutase from dog (Canis familiaris) complexed with 19A9 triabody in the closed conformation
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| D | 0004784 | molecular_function | superoxide dismutase activity |
| D | 0005507 | molecular_function | copper ion binding |
| D | 0005634 | cellular_component | nucleus |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005739 | cellular_component | mitochondrion |
| D | 0005777 | cellular_component | peroxisome |
| D | 0005829 | cellular_component | cytosol |
| D | 0019430 | biological_process | removal of superoxide radicals |
| D | 0072593 | biological_process | reactive oxygen species metabolic process |
| E | 0004784 | molecular_function | superoxide dismutase activity |
| E | 0005507 | molecular_function | copper ion binding |
| E | 0005634 | cellular_component | nucleus |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0005739 | cellular_component | mitochondrion |
| E | 0005777 | cellular_component | peroxisome |
| E | 0005829 | cellular_component | cytosol |
| E | 0019430 | biological_process | removal of superoxide radicals |
| E | 0072593 | biological_process | reactive oxygen species metabolic process |
| F | 0004784 | molecular_function | superoxide dismutase activity |
| F | 0005507 | molecular_function | copper ion binding |
| F | 0005634 | cellular_component | nucleus |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0005739 | cellular_component | mitochondrion |
| F | 0005777 | cellular_component | peroxisome |
| F | 0005829 | cellular_component | cytosol |
| F | 0019430 | biological_process | removal of superoxide radicals |
| F | 0072593 | biological_process | reactive oxygen species metabolic process |
Functional Information from PROSITE/UniProt
| site_id | PS00332 |
| Number of Residues | 12 |
| Details | SOD_CU_ZN_2 Copper/Zinc superoxide dismutase signature 2. GNAGsRlACgvI |
| Chain | Residue | Details |
| D | GLY138-ILE149 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 21 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P00441","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P08228","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P00441","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P08228","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P00441","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"UniProtKB","id":"P00441","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
