Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004517 | molecular_function | nitric-oxide synthase activity |
A | 0005575 | cellular_component | cellular_component |
A | 0006809 | biological_process | nitric oxide biosynthetic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0020037 | molecular_function | heme binding |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE HEM A 901 |
Chain | Residue |
A | TRP60 |
A | TYR355 |
A | TYR357 |
A | H4B902 |
A | PQW904 |
A | GOL905 |
A | HOH2318 |
A | HOH2319 |
A | SER63 |
A | ARG65 |
A | CYS66 |
A | PHE235 |
A | ASN236 |
A | TRP238 |
A | GLU243 |
A | TRP329 |
site_id | AC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE H4B A 902 |
Chain | Residue |
A | ARG247 |
A | TRP327 |
A | THR328 |
A | TRP329 |
A | PHE342 |
A | HIS343 |
A | ARG344 |
A | HEM901 |
A | HOH2219 |
A | HOH2296 |
A | HOH2303 |
A | HOH2319 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 903 |
Chain | Residue |
A | GLN129 |
A | TYR239 |
A | ASN248 |
site_id | AC4 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE PQW A 904 |
Chain | Residue |
A | HIS128 |
A | PRO216 |
A | ILE218 |
A | PHE235 |
A | ASN236 |
A | GLY237 |
A | TRP238 |
A | GLU243 |
A | TRP329 |
A | TYR357 |
A | GLN358 |
A | LYS360 |
A | HEM901 |
A | HOH2203 |
A | HOH2315 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 905 |
Chain | Residue |
A | MET221 |
A | TYR355 |
A | PHE356 |
A | TYR357 |
A | HEM901 |
A | HOH2046 |
A | HOH2320 |
Functional Information from PROSITE/UniProt
site_id | PS60001 |
Number of Residues | 8 |
Details | NOS Nitric oxide synthase (NOS) signature. RCIGRLfW |
Chain | Residue | Details |
A | ARG65-TRP72 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | BINDING: axial binding residue |
Chain | Residue | Details |
A | CYS66 | |