Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004517 | molecular_function | nitric-oxide synthase activity |
| 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 | 18 |
| Details | BINDING SITE FOR RESIDUE HEM A 901 |
| Chain | Residue |
| A | TRP60 |
| A | TRP329 |
| A | TYR355 |
| A | TYR357 |
| A | H4B902 |
| A | JHT904 |
| A | GOL905 |
| A | HOH2189 |
| A | HOH2200 |
| A | HOH2300 |
| A | SER63 |
| A | ARG65 |
| A | CYS66 |
| A | PHE235 |
| A | ASN236 |
| A | GLY237 |
| A | TRP238 |
| A | GLU243 |
| site_id | AC2 |
| Number of Residues | 9 |
| 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 | HOH2277 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 903 |
| Chain | Residue |
| A | GLN129 |
| A | ARG132 |
| A | TYR239 |
| A | ASN248 |
| A | HOH2108 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE JHT A 904 |
| Chain | Residue |
| A | HIS128 |
| A | TRP238 |
| A | TYR239 |
| A | GLU243 |
| A | HEM901 |
| A | HOH2189 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 905 |
| Chain | Residue |
| A | MET221 |
| A | PHE356 |
| A | TYR357 |
| A | HEM901 |
| A | HOH2035 |
| A | HOH2302 |
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 site: {"description":"axial binding residue"} |
