2ALL
Crystal structure of L122V/L132V mutant of nitrophorin 2
Functional Information from GO Data
Chain | GOid | namespace | contents |
X | 0005576 | cellular_component | extracellular region |
X | 0035821 | biological_process | modulation of process of another organism |
X | 0042311 | biological_process | vasodilation |
X | 0046872 | molecular_function | metal ion binding |
X | 0051381 | molecular_function | histamine binding |
X | 0070026 | molecular_function | nitric oxide binding |
X | 0090729 | molecular_function | toxin activity |
X | 0097746 | biological_process | blood vessel diameter maintenance |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE HEM X 201 |
Chain | Residue |
X | PHE27 |
X | ILE120 |
X | VAL122 |
X | HOH259 |
X | HOH275 |
X | HOH380 |
X | HOH388 |
X | TYR38 |
X | LEU55 |
X | HIS57 |
X | ASN68 |
X | TYR85 |
X | THR87 |
X | TYR104 |
X | LEU106 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | Binding site: {"description":"proximal binding residue","evidences":[{"source":"PubMed","id":"10884386","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EUO","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |