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 |
