1FVA
CRYSTAL STRUCTURE OF BOVINE METHIONINE SULFOXIDE REDUCTASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0008113 | molecular_function | peptide-methionine (S)-S-oxide reductase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0033744 | molecular_function | L-methionine (S)-S-oxide reductase activity |
| A | 0034599 | biological_process | cellular response to oxidative stress |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0008113 | molecular_function | peptide-methionine (S)-S-oxide reductase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0033744 | molecular_function | L-methionine (S)-S-oxide reductase activity |
| B | 0034599 | biological_process | cellular response to oxidative stress |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Cysteine sulfenic acid (-SOH) intermediate","evidences":[{"source":"UniProtKB","id":"P0A744","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9D6Y7","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | a catalytic site defined by CSA, PubMed 11063566, 10841552 |
| Chain | Residue | Details |
| A | CYS72 | |
| A | CYS218 | |
| A | CYS227 | |
| A | GLU115 | |
| A | TYR103 |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 122 |
| Chain | Residue | Details |
| A | CYS72 | covalently attached, electrofuge, electrophile, nucleofuge, nucleophile |
| A | TYR103 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
| A | GLU115 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ASP150 | proton acceptor, proton donor, proton relay |
| A | TYR155 | electrostatic stabiliser, hydrogen bond donor |
| A | CYS218 | electrofuge, electrophile, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
| A | CYS227 | electrofuge, electrophile, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 122 |
| Chain | Residue | Details |
| B | CYS72 | covalently attached, electrofuge, electrophile, nucleofuge, nucleophile |
| B | TYR103 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
| B | GLU115 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | ASP150 | proton acceptor, proton donor, proton relay |
| B | TYR155 | electrostatic stabiliser, hydrogen bond donor |
| B | CYS218 | electrofuge, electrophile, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
| B | CYS227 | electrofuge, electrophile, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
