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 | 6 |
| Details | BINDING SITE FOR RESIDUE ACT A 1850 |
| Chain | Residue |
| A | GLN249 |
| A | ARG252 |
| A | ASN368 |
| A | ARG374 |
| A | HOH2912 |
| A | HOH3088 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACT A 1860 |
| Chain | Residue |
| A | HEM1500 |
| A | HOH2920 |
| A | HOH2989 |
| A | HOH3012 |
| A | TRP358 |
| A | VAL420 |
| A | SER428 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT B 2850 |
| Chain | Residue |
| B | ARG252 |
| B | ASN368 |
| B | ARG374 |
| B | HOH2958 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACT B 2860 |
| Chain | Residue |
| B | GLY188 |
| B | TRP358 |
| B | VAL420 |
| B | SER428 |
| B | HOH2978 |
| B | HOH3053 |
| B | HOH3074 |
| B | HOH3208 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 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 1500 |
| Chain | Residue |
| A | TRP180 |
| A | ARG185 |
| A | CYS186 |
| A | SER228 |
| A | PHE355 |
| A | SER356 |
| A | TRP358 |
| A | GLU363 |
| A | TRP449 |
| A | TYR477 |
| A | IPU1830 |
| A | ACT1860 |
| A | HOH2942 |
| A | HOH2951 |
| A | HOH2995 |
| A | HOH3044 |
| A | HOH3155 |
| B | HOH3032 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE IPU A 1830 |
| Chain | Residue |
| A | PRO336 |
| A | VAL338 |
| A | PHE355 |
| A | SER356 |
| A | TRP358 |
| A | GLU363 |
| A | HEM1500 |
| A | HOH2894 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE IPU B 1840 |
| Chain | Residue |
| A | VAL106 |
| A | ALA448 |
| A | TRP449 |
| B | TRP447 |
| B | PHE462 |
| B | HIS463 |
| B | GOL1880 |
| B | HOH3032 |
| B | HOH3086 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CAD A 1950 |
| Chain | Residue |
| A | TRP324 |
| A | CYS384 |
| site_id | BC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEM B 2500 |
| Chain | Residue |
| A | HOH2971 |
| B | TRP180 |
| B | ARG185 |
| B | CYS186 |
| B | SER228 |
| B | PHE355 |
| B | SER356 |
| B | TRP358 |
| B | GLU363 |
| B | TRP449 |
| B | TYR477 |
| B | IPU2830 |
| B | HOH2960 |
| B | HOH3019 |
| B | HOH3026 |
| B | HOH3033 |
| B | HOH3070 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE IPU B 2830 |
| Chain | Residue |
| B | PRO336 |
| B | PHE355 |
| B | SER356 |
| B | TRP358 |
| B | TYR359 |
| B | GLU363 |
| B | HEM2500 |
| site_id | BC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE IPU A 2840 |
| Chain | Residue |
| B | ALA448 |
| B | TRP449 |
| A | TRP447 |
| A | PHE462 |
| A | HIS463 |
| A | GOL2880 |
| A | HOH2939 |
| A | HOH2971 |
| A | HOH2994 |
| A | HOH3152 |
| B | SER104 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CAD B 2950 |
| Chain | Residue |
| B | TYR83 |
| B | TRP324 |
| B | CYS384 |
| site_id | BC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 1880 |
| Chain | Residue |
| A | ARG367 |
| A | ALA448 |
| A | TRP449 |
| B | PHE462 |
| B | IPU1840 |
| B | HOH3024 |
| B | HOH3032 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 1885 |
| Chain | Residue |
| A | VAL263 |
| A | GLY265 |
| A | PRO267 |
| A | ARG287 |
| A | TYR375 |
| A | HOH3078 |
| site_id | BC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 2880 |
| Chain | Residue |
| A | PHE462 |
| A | HIS463 |
| A | IPU2840 |
| A | HOH2939 |
| A | HOH2971 |
| A | HOH3152 |
| B | SER104 |
| B | VAL106 |
| B | TRP449 |
| site_id | BC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 2885 |
| Chain | Residue |
| B | VAL263 |
| B | GLY265 |
| B | PRO267 |
| B | ARG287 |
| B | ARG374 |
| B | TYR375 |
| B | HOH3221 |
| B | HOH3222 |
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 | |
