3HCH
Structure of the C-terminal domain (MsrB) of Neisseria meningitidis PilB (complex with substrate)
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 RSM A 1000 |
Chain | Residue |
A | HOH20 |
A | TRP442 |
A | ARG466 |
A | GLY479 |
A | HIS480 |
A | PHE482 |
A | ARG493 |
A | SER495 |
site_id | AC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE RSM A 1001 |
Chain | Residue |
A | HOH109 |
A | TYR436 |
A | ASP437 |
A | SER438 |
A | LYS489 |
B | HOH4 |
B | TYR436 |
B | ASP437 |
B | SER438 |
B | ASP484 |
B | LYS489 |
B | P6G1009 |
A | HOH46 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CIT A 1003 |
Chain | Residue |
A | ALA433 |
A | ASP434 |
A | LYS435 |
A | TYR436 |
A | LYS489 |
B | ASP488 |
B | LYS489 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE P6G A 1005 |
Chain | Residue |
A | GLU456 |
A | ARG465 |
A | THR467 |
A | PHE482 |
A | PRO483 |
A | ASP484 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE RSM B 1000 |
Chain | Residue |
B | HOH110 |
B | TRP442 |
B | ARG466 |
B | GLY479 |
B | HIS480 |
B | PHE482 |
B | SER495 |
B | P6G1008 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE TRS B 1002 |
Chain | Residue |
A | PRO417 |
A | GLU507 |
B | HOH95 |
B | ALA451 |
B | VAL454 |
B | THR455 |
B | GLU456 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE P6G B 1004 |
Chain | Residue |
B | THR389 |
B | GLN394 |
B | VAL423 |
B | LYS502 |
B | ALA512 |
B | TYR514 |
B | P6G1007 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE P6G B 1007 |
Chain | Residue |
B | LYS416 |
B | PRO417 |
B | PHE503 |
B | GLN508 |
B | ALA511 |
B | P6G1004 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE P6G B 1008 |
Chain | Residue |
B | ARG465 |
B | THR467 |
B | VAL481 |
B | PRO483 |
B | ASP484 |
B | ARG493 |
B | RSM1000 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE P6G B 1009 |
Chain | Residue |
A | SER438 |
A | RSM1001 |
B | SER438 |
B | ASP484 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 123 |
Details | Domain: {"description":"MsrB","evidences":[{"source":"PROSITE-ProRule","id":"PRU01126","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU01126","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |