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 | 14 |
Details | BINDING SITE FOR RESIDUE HEM A 501 |
Chain | Residue |
A | TRP180 |
A | TYR477 |
A | H4B502 |
A | QJ8503 |
A | HOH644 |
A | HOH706 |
A | CYS186 |
A | SER228 |
A | PHE355 |
A | SER356 |
A | TRP358 |
A | GLU363 |
A | TRP449 |
A | PHE475 |
site_id | AC2 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE H4B A 502 |
Chain | Residue |
A | SER104 |
A | ARG367 |
A | ALA448 |
A | TRP449 |
A | HEM501 |
A | GOL506 |
A | HOH677 |
A | HOH705 |
A | HOH706 |
B | TRP447 |
B | PHE462 |
B | HIS463 |
B | GLN464 |
B | GLU465 |
B | HOH716 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE QJ8 A 503 |
Chain | Residue |
A | VAL338 |
A | ASN340 |
A | PHE355 |
A | TRP358 |
A | TYR359 |
A | GLU363 |
A | TYR477 |
A | HEM501 |
A | HOH749 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACT A 504 |
Chain | Residue |
A | TRP358 |
A | VAL420 |
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 | HOH687 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 506 |
Chain | Residue |
A | ARG367 |
A | HIS373 |
A | H4B502 |
A | HOH749 |
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 | 15 |
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 | TYR477 |
B | H4B502 |
B | QJ8503 |
B | HOH624 |
B | HOH660 |
B | HOH682 |
B | HOH726 |
site_id | AC9 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE H4B B 502 |
Chain | Residue |
A | TRP447 |
A | PHE462 |
A | HOH657 |
B | SER104 |
B | ARG367 |
B | ALA448 |
B | TRP449 |
B | HEM501 |
B | GOL506 |
B | HOH624 |
B | HOH730 |
B | HOH743 |
site_id | BC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE QJ8 B 503 |
Chain | Residue |
A | TRP76 |
B | VAL106 |
B | LEU107 |
B | VAL338 |
B | TRP358 |
B | TYR359 |
B | GLU363 |
B | HEM501 |
B | ACT505 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT B 504 |
Chain | Residue |
B | ILE190 |
B | TRP358 |
B | VAL420 |
B | SER428 |
B | HOH669 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACT B 505 |
Chain | Residue |
B | QJ8503 |
B | HOH745 |
B | GLN249 |
B | ARG252 |
B | ASN368 |
B | ARG374 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL B 506 |
Chain | Residue |
B | VAL106 |
B | ARG367 |
B | HIS373 |
B | H4B502 |
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 | |