4GRJ
Crystal structure of nitrophorin 4 triple mutant complex with NO
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005576 | cellular_component | extracellular region |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0042311 | biological_process | vasodilation |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051381 | molecular_function | histamine binding |
| A | 0070026 | molecular_function | nitric oxide binding |
| A | 0097746 | biological_process | blood vessel diameter maintenance |
| B | 0005576 | cellular_component | extracellular region |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0042311 | biological_process | vasodilation |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051381 | molecular_function | histamine binding |
| B | 0070026 | molecular_function | nitric oxide binding |
| B | 0097746 | biological_process | blood vessel diameter maintenance |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEM A 201 |
| Chain | Residue |
| A | VAL25 |
| A | LYS88 |
| A | TYR105 |
| A | PHE107 |
| A | LEU123 |
| A | LYS125 |
| A | LEU130 |
| A | LEU133 |
| A | NO202 |
| A | HOH414 |
| A | HOH427 |
| A | TYR28 |
| A | VAL36 |
| A | TYR40 |
| A | LEU57 |
| A | HIS59 |
| A | PHE68 |
| A | ASP70 |
| A | PHE86 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NO A 202 |
| Chain | Residue |
| A | LEU130 |
| A | LEU133 |
| A | HEM201 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A 203 |
| Chain | Residue |
| A | PRO37 |
| A | LYS38 |
| A | ARG39 |
| A | LYS63 |
| A | HOH347 |
| A | HOH372 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEM B 201 |
| Chain | Residue |
| B | VAL25 |
| B | TYR28 |
| B | VAL36 |
| B | PRO37 |
| B | TYR40 |
| B | ALA42 |
| B | LEU57 |
| B | HIS59 |
| B | PHE68 |
| B | ASP70 |
| B | PHE86 |
| B | LYS88 |
| B | TYR105 |
| B | PHE107 |
| B | LEU123 |
| B | LYS125 |
| B | LEU130 |
| B | LEU133 |
| B | NO202 |
| B | HOH354 |
| B | HOH474 |
| B | HOH500 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NO B 202 |
| Chain | Residue |
| B | LEU123 |
| B | HEM201 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 B 203 |
| Chain | Residue |
| A | ALA1 |
| A | GLN32 |
| A | HOH401 |
| A | HOH443 |
| B | ALA145 |
| B | GLY146 |
| B | LYS150 |
| B | HOH396 |
| B | HOH398 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"proximal binding residue","evidences":[{"source":"PubMed","id":"10876239","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11560480","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14673714","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16171383","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20524697","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22334402","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22976968","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23474537","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9782054","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
