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 | 3 |
Details | BINDING SITE FOR RESIDUE ACT B 2860 |
Chain | Residue |
B | GLY188 |
B | TRP358 |
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 | ARG185 |
A | CYS186 |
A | SER228 |
A | PHE355 |
A | SER356 |
A | TRP358 |
A | GLU363 |
A | TRP449 |
A | TYR477 |
A | ARG1700 |
A | HOH1956 |
A | HOH2009 |
A | HOH2028 |
A | HOH2040 |
A | HOH2063 |
A | HOH2083 |
A | HOH2124 |
site_id | AC7 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE HEM B 500 |
Chain | Residue |
B | TRP180 |
B | ARG185 |
B | CYS186 |
B | SER228 |
B | PHE355 |
B | SER356 |
B | TRP358 |
B | GLU363 |
B | TRP449 |
B | TYR477 |
B | ARG2700 |
B | GOL2885 |
B | HOH2962 |
B | HOH2972 |
B | HOH3059 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ARG A 1700 |
Chain | Residue |
A | GLN249 |
A | TRP358 |
A | TYR359 |
A | GLU363 |
A | ASN368 |
A | HEM500 |
A | HOH1967 |
A | HOH2047 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ARG B 2700 |
Chain | Residue |
B | GLN249 |
B | TRP358 |
B | TYR359 |
B | GLU363 |
B | ASN368 |
B | HEM500 |
B | HOH3022 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 1880 |
Chain | Residue |
A | ARG367 |
A | HIS373 |
A | HOH1974 |
B | HOH2955 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL B 2880 |
Chain | Residue |
B | ARG367 |
B | HIS373 |
B | GOL2885 |
B | HOH2990 |
site_id | BC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 2885 |
Chain | Residue |
A | PHE462 |
B | ARG367 |
B | ALA448 |
B | TRP449 |
B | HEM500 |
B | GOL2880 |
B | HOH3062 |
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 | |