1L1D
Crystal structure of the C-terminal methionine sulfoxide reductase domain (MsrB) of N. gonorrhoeae pilB
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006979 | biological_process | response to oxidative stress |
A | 0016671 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor |
A | 0030091 | biological_process | protein repair |
A | 0033743 | molecular_function | peptide-methionine (R)-S-oxide reductase activity |
B | 0006979 | biological_process | response to oxidative stress |
B | 0016671 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor |
B | 0030091 | biological_process | protein repair |
B | 0033743 | molecular_function | peptide-methionine (R)-S-oxide reductase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE CAC A 601 |
Chain | Residue |
A | HOH1 |
A | HOH110 |
A | HOH112 |
A | THR403 |
A | TRP442 |
A | GLY479 |
A | HIS480 |
A | CYS495 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CAC B 602 |
Chain | Residue |
A | GLU393 |
A | ALA402 |
A | THR403 |
A | TYR405 |
B | LYS387 |
A | HOH105 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CAC B 603 |
Chain | Residue |
A | LYS387 |
B | HOH34 |
B | HOH43 |
B | GLU393 |
B | ALA402 |
B | THR403 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU01126 |
Chain | Residue | Details |
A | CYS495 | |
B | CYS495 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 5 |
Details | a catalytic site defined by CSA, PubMed 11938352, 11812798, 15350148 |
Chain | Residue | Details |
A | HIS480 | |
A | ARG493 | |
A | CYS495 | |
A | CYS440 | |
A | ASP484 |
site_id | CSA2 |
Number of Residues | 5 |
Details | a catalytic site defined by CSA, PubMed 11938352, 11812798, 15350148 |
Chain | Residue | Details |
B | HIS480 | |
B | ARG493 | |
B | CYS495 | |
B | CYS440 | |
B | ASP484 |
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 715 |
Chain | Residue | Details |
A | CYS440 | nucleofuge, nucleophile, proton acceptor |
A | HIS477 | proton acceptor, proton donor |
A | HIS480 | electrostatic stabiliser, proton acceptor, proton donor |
A | ASP484 | electrostatic stabiliser |
A | ARG493 | electrostatic stabiliser |
A | CYS495 | covalently attached, electrofuge, electrophile, nucleofuge, nucleophile |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 715 |
Chain | Residue | Details |
B | CYS440 | nucleofuge, nucleophile, proton acceptor |
B | HIS477 | proton acceptor, proton donor |
B | HIS480 | electrostatic stabiliser, proton acceptor, proton donor |
B | ASP484 | electrostatic stabiliser |
B | ARG493 | electrostatic stabiliser |
B | CYS495 | covalently attached, electrofuge, electrophile, nucleofuge, nucleophile |