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 | 15 |
Details | binding site for residue HEM A 501 |
Chain | Residue |
A | TRP180 |
A | TRP449 |
A | PHE475 |
A | TYR477 |
A | H4B502 |
A | P94503 |
A | HOH602 |
A | ALA183 |
A | CYS186 |
A | SER228 |
A | PHE355 |
A | SER356 |
A | TRP358 |
A | MET360 |
A | GLU363 |
site_id | AC2 |
Number of Residues | 10 |
Details | binding site for residue H4B A 502 |
Chain | Residue |
A | SER104 |
A | ARG367 |
A | ALA448 |
A | TRP449 |
A | HEM501 |
A | GOL506 |
A | HOH602 |
B | TRP447 |
B | PHE462 |
B | HOH602 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue P94 A 503 |
Chain | Residue |
A | VAL106 |
A | LEU107 |
A | VAL338 |
A | TRP358 |
A | GLU363 |
A | TRP449 |
A | TYR477 |
A | HEM501 |
B | TRP76 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue ACT A 504 |
Chain | Residue |
A | TRP358 |
A | SER428 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue ACT A 505 |
Chain | Residue |
A | ARG252 |
A | ASN368 |
A | ARG374 |
A | HOH632 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue GOL A 506 |
Chain | Residue |
A | VAL106 |
A | ARG367 |
A | HIS373 |
A | H4B502 |
B | TRP76 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue ZN A 507 |
Chain | Residue |
A | CYS96 |
A | CYS101 |
B | CYS96 |
B | CYS101 |
site_id | AC8 |
Number of Residues | 12 |
Details | binding site for residue HEM B 501 |
Chain | Residue |
B | TRP180 |
B | ARG185 |
B | CYS186 |
B | SER228 |
B | PHE355 |
B | SER356 |
B | TRP358 |
B | GLU363 |
B | TRP449 |
B | TYR477 |
B | H4B502 |
B | P94503 |
site_id | AC9 |
Number of Residues | 9 |
Details | binding site for residue H4B B 502 |
Chain | Residue |
A | TRP447 |
A | PHE462 |
A | GLU465 |
B | SER104 |
B | ARG367 |
B | ALA448 |
B | TRP449 |
B | HEM501 |
B | GOL506 |
site_id | AD1 |
Number of Residues | 9 |
Details | binding site for residue P94 B 503 |
Chain | Residue |
A | TRP76 |
B | LEU107 |
B | VAL338 |
B | TRP358 |
B | GLU363 |
B | TRP449 |
B | TYR477 |
B | HEM501 |
B | GOL506 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue ACT B 504 |
Chain | Residue |
B | TRP358 |
B | VAL420 |
B | SER428 |
B | HOH628 |
site_id | AD3 |
Number of Residues | 5 |
Details | binding site for residue ACT B 505 |
Chain | Residue |
B | GLN249 |
B | ARG252 |
B | ASN368 |
B | ARG374 |
B | HOH613 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue GOL B 506 |
Chain | Residue |
B | VAL106 |
B | ARG367 |
B | HIS373 |
B | H4B502 |
B | P94503 |
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
Chain | Residue | Details |
A | CYS96 | |
A | CYS101 | |
B | CYS96 | |
B | CYS101 | |
Chain | Residue | Details |
A | SER104 | |
A | TYR477 | |
B | SER104 | |
B | GLN249 | |
B | TRP358 | |
B | TYR359 | |
B | GLU363 | |
B | ASN368 | |
B | ALA448 | |
B | TRP449 | |
B | PHE462 | |
A | GLN249 | |
B | TYR477 | |
A | TRP358 | |
A | TYR359 | |
A | GLU363 | |
A | ASN368 | |
A | ALA448 | |
A | TRP449 | |
A | PHE462 | |
Chain | Residue | Details |
A | CYS186 | |
B | CYS186 | |
Chain | Residue | Details |
A | SER116 | |
B | SER116 | |