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 |
| B | 0004517 | molecular_function | nitric-oxide synthase activity |
| B | 0006809 | biological_process | nitric oxide biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CAC A 1950 |
| Chain | Residue |
| A | TRP324 |
| A | CYS384 |
| A | LYS438 |
| A | ARG440 |
| A | GLY441 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CAC B 2950 |
| Chain | Residue |
| B | TYR83 |
| B | TRP324 |
| B | CYS384 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT A 1860 |
| Chain | Residue |
| A | TRP358 |
| A | SER428 |
| A | GLY188 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT B 2860 |
| Chain | Residue |
| B | GLY188 |
| B | ILE190 |
| B | GLN191 |
| B | TRP358 |
| B | VAL420 |
| B | SER428 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 900 |
| Chain | Residue |
| A | CYS96 |
| A | CYS101 |
| B | CYS96 |
| B | CYS101 |
| site_id | AC6 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEM A 500 |
| Chain | Residue |
| A | TRP180 |
| A | CYS186 |
| A | VAL187 |
| A | SER228 |
| A | MET341 |
| A | PHE355 |
| A | SER356 |
| A | TRP358 |
| A | GLU363 |
| A | TRP449 |
| A | PHE475 |
| A | TYR477 |
| A | H4B1600 |
| A | ARG1700 |
| A | NO1910 |
| A | HOH1961 |
| A | HOH2037 |
| A | HOH2070 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NO A 1910 |
| Chain | Residue |
| A | PHE355 |
| A | HEM500 |
| A | ARG1700 |
| site_id | AC8 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEM B 500 |
| Chain | Residue |
| B | TRP180 |
| B | ARG185 |
| B | CYS186 |
| B | VAL187 |
| B | SER228 |
| B | MET341 |
| B | PHE355 |
| B | SER356 |
| B | TRP358 |
| B | GLU363 |
| B | TRP449 |
| B | TYR477 |
| B | H4B2600 |
| B | ARG2700 |
| B | NO2910 |
| B | HOH2952 |
| B | HOH2961 |
| B | HOH2970 |
| B | HOH3041 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NO B 2910 |
| Chain | Residue |
| B | HEM500 |
| B | ARG2700 |
| site_id | BC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE H4B A 1600 |
| Chain | Residue |
| A | SER104 |
| A | ARG367 |
| A | ALA448 |
| A | TRP449 |
| A | HEM500 |
| A | GOL1880 |
| A | HOH1963 |
| A | HOH1975 |
| A | HOH2035 |
| B | TRP447 |
| B | PHE462 |
| B | HIS463 |
| B | GLN464 |
| B | GLU465 |
| B | HOH3058 |
| site_id | BC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE H4B B 2600 |
| Chain | Residue |
| A | TRP447 |
| A | PHE462 |
| A | GLU465 |
| B | SER104 |
| B | ARG367 |
| B | ALA448 |
| B | TRP449 |
| B | HEM500 |
| B | GOL2880 |
| B | HOH2966 |
| B | HOH2968 |
| B | HOH3041 |
| B | HOH3078 |
| site_id | BC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ARG A 1700 |
| Chain | Residue |
| A | NO1910 |
| A | HOH1973 |
| A | GLN249 |
| A | TYR333 |
| A | PRO336 |
| A | TRP358 |
| A | TYR359 |
| A | GLU363 |
| A | ASN368 |
| A | HEM500 |
| site_id | BC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ARG B 2700 |
| Chain | Residue |
| B | GLN249 |
| B | ARG252 |
| B | PRO336 |
| B | TRP358 |
| B | TYR359 |
| B | GLU363 |
| B | ASN368 |
| B | HEM500 |
| B | NO2910 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 1880 |
| Chain | Residue |
| A | ARG367 |
| A | HIS373 |
| A | H4B1600 |
| A | HOH2091 |
| B | TRP76 |
| B | HOH3058 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 2880 |
| Chain | Residue |
| B | VAL106 |
| B | ARG367 |
| B | HIS373 |
| B | H4B2600 |
| B | HOH3078 |
Functional Information from PROSITE/UniProt
| site_id | PS60001 |
| Number of Residues | 8 |
| Details | NOS Nitric oxide synthase (NOS) signature. RCVGRIqW |
| Chain | Residue | Details |
| A | ARG185-TRP192 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P35228","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P29474","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"UniProtKB","id":"P29474","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by CDK5","evidences":[{"source":"UniProtKB","id":"P29474","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 | CYS186 | |
| A | ARG189 | |
| A | GLU363 | |
| A | TRP358 | |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 3nos |
| Chain | Residue | Details |
| B | CYS186 | |
| B | ARG189 | |
| B | GLU363 | |
| B | TRP358 | |
