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 | 0020037 | molecular_function | heme binding |
| B | 0004517 | molecular_function | nitric-oxide synthase activity |
| B | 0006809 | biological_process | nitric oxide biosynthetic process |
| B | 0020037 | molecular_function | heme binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT A 860 |
| Chain | Residue |
| A | GLY417 |
| A | TRP587 |
| A | SER657 |
| A | HEM750 |
| A | HOH1059 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT B 1860 |
| Chain | Residue |
| B | HOH2161 |
| B | GLN420 |
| B | TRP587 |
| B | HOH1956 |
| B | HOH2113 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 900 |
| Chain | Residue |
| A | CYS326 |
| A | CYS331 |
| B | CYS326 |
| B | CYS331 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE HEM A 750 |
| Chain | Residue |
| A | TRP409 |
| A | CYS415 |
| A | SER457 |
| A | PHE584 |
| A | SER585 |
| A | GLY586 |
| A | TRP587 |
| A | GLU592 |
| A | TRP678 |
| A | TYR706 |
| A | H4B760 |
| A | BHH831 |
| A | ACT860 |
| A | HOH905 |
| A | HOH907 |
| A | HOH918 |
| A | HOH973 |
| A | HOH980 |
| A | HOH986 |
| A | HOH1060 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE H4B A 760 |
| Chain | Residue |
| A | SER334 |
| A | MET336 |
| A | ARG596 |
| A | VAL677 |
| A | TRP678 |
| A | HEM750 |
| A | HOH902 |
| A | HOH905 |
| A | HOH917 |
| A | HOH936 |
| A | HOH1028 |
| B | TRP676 |
| B | PHE691 |
| B | HIS692 |
| B | GLN693 |
| B | GLU694 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE BHH A 831 |
| Chain | Residue |
| A | GLN478 |
| A | PRO565 |
| A | ALA566 |
| A | GLY586 |
| A | TRP587 |
| A | GLU592 |
| A | HEM750 |
| A | HOH914 |
| A | HOH1060 |
| site_id | AC7 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE HEM B 750 |
| Chain | Residue |
| B | TRP409 |
| B | CYS415 |
| B | PHE584 |
| B | SER585 |
| B | TRP587 |
| B | GLU592 |
| B | TRP678 |
| B | TYR706 |
| B | H4B1760 |
| B | BHH1831 |
| B | HOH1872 |
| B | HOH1892 |
| B | HOH1942 |
| B | HOH1962 |
| B | HOH1988 |
| B | HOH2079 |
| site_id | AC8 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE H4B B 1760 |
| Chain | Residue |
| A | TRP676 |
| A | PHE691 |
| A | HIS692 |
| A | GLN693 |
| A | GLU694 |
| B | SER334 |
| B | MET336 |
| B | ARG596 |
| B | VAL677 |
| B | TRP678 |
| B | HEM750 |
| B | HOH1861 |
| B | HOH1886 |
| B | HOH1892 |
| B | HOH1941 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE BHH B 1831 |
| Chain | Residue |
| B | GLN478 |
| B | PRO565 |
| B | VAL567 |
| B | GLY586 |
| B | TRP587 |
| B | GLU592 |
| B | HEM750 |
| B | HOH1873 |
| B | HOH1879 |
Functional Information from PROSITE/UniProt
| site_id | PS60001 |
| Number of Residues | 8 |
| Details | NOS Nitric oxide synthase (NOS) signature. RCVGRIqW |
| Chain | Residue | Details |
| A | ARG414-TRP421 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P29475","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"UniProtKB","id":"P29475","evidenceCode":"ECO:0000250"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 3nos |
| Chain | Residue | Details |
| A | CYS415 | |
| A | TRP587 | |
| A | GLU592 | |
| A | ARG418 | |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 3nos |
| Chain | Residue | Details |
| B | CYS415 | |
| B | TRP587 | |
| B | GLU592 | |
| B | ARG418 | |
