1FF3
STRUCTURE OF THE PEPTIDE METHIONINE SULFOXIDE REDUCTASE FROM ESCHERICHIA COLI
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0008113 | molecular_function | peptide-methionine (S)-S-oxide reductase activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016671 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor |
| A | 0030091 | biological_process | protein repair |
| 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 | 0005829 | cellular_component | cytosol |
| B | 0006979 | biological_process | response to oxidative stress |
| B | 0008113 | molecular_function | peptide-methionine (S)-S-oxide reductase activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016671 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor |
| B | 0030091 | biological_process | protein repair |
| B | 0033744 | molecular_function | L-methionine (S)-S-oxide reductase activity |
| B | 0034599 | biological_process | cellular response to oxidative stress |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006979 | biological_process | response to oxidative stress |
| C | 0008113 | molecular_function | peptide-methionine (S)-S-oxide reductase activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016671 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor |
| C | 0030091 | biological_process | protein repair |
| C | 0033744 | molecular_function | L-methionine (S)-S-oxide reductase activity |
| C | 0034599 | biological_process | cellular response to oxidative stress |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 533 |
| Chain | Residue |
| A | THR81 |
| A | ARG83 |
| A | HOH602 |
| A | HOH639 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 534 |
| Chain | Residue |
| A | SER1 |
| A | LYS5 |
| A | LYS6 |
| A | HIS7 |
| B | HIS7 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 535 |
| Chain | Residue |
| A | ARG18 |
| A | ASN19 |
| A | THR20 |
| A | HOH759 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 536 |
| Chain | Residue |
| B | ARG18 |
| B | ASN19 |
| B | THR20 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Cysteine sulfenic acid (-SOH) intermediate","evidences":[{"source":"PubMed","id":"10964927","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 11080639, 10964927 |
| Chain | Residue | Details |
| A | CAS51 | |
| A | CYS198 | |
| A | CYS206 | |
| A | GLU94 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 11080639, 10964927 |
| Chain | Residue | Details |
| A | CAS51 | |
| A | CYS198 | |
| A | CYS206 | |
| A | GLU94 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | a catalytic site defined by CSA, PubMed 11080639, 10964927 |
| Chain | Residue | Details |
| B | GLU94 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | a catalytic site defined by CSA, PubMed 11080639, 10964927 |
| Chain | Residue | Details |
| C | GLU94 |
