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 500 |
Chain | Residue |
A | TRP180 |
A | XFJ800 |
A | HOH1004 |
A | HOH1045 |
A | HOH1073 |
A | HOH1143 |
A | CYS186 |
A | SER228 |
A | PHE355 |
A | SER356 |
A | TRP358 |
A | GLU363 |
A | TRP449 |
A | H4B600 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACT A 860 |
Chain | Residue |
A | GLY188 |
A | TRP358 |
A | SER428 |
A | HOH1152 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CAD A 950 |
Chain | Residue |
A | TRP324 |
A | LEU328 |
A | CYS384 |
A | HOH1132 |
site_id | AC4 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE H4B A 600 |
Chain | Residue |
A | SER104 |
A | ARG367 |
A | ALA448 |
A | TRP449 |
A | HEM500 |
A | HOH1030 |
A | HOH1038 |
A | HOH1045 |
A | HOH1140 |
A | HOH1164 |
B | TRP447 |
B | PHE462 |
B | HIS463 |
B | GLN464 |
B | GLU465 |
site_id | AC5 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE XFJ A 800 |
Chain | Residue |
A | MET106 |
A | ARG185 |
A | GLN249 |
A | VAL338 |
A | PHE355 |
A | TRP358 |
A | GLU363 |
A | HEM500 |
A | HOH1004 |
A | HOH1111 |
B | TRP76 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 900 |
Chain | Residue |
A | CYS96 |
A | CYS101 |
B | CYS96 |
B | CYS101 |
site_id | AC7 |
Number of Residues | 14 |
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 | H4B600 |
B | XFJ800 |
B | HOH1225 |
B | HOH1262 |
B | HOH1301 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT B 860 |
Chain | Residue |
B | TRP358 |
B | SER428 |
B | HOH1343 |
B | HOH1363 |
B | HOH1415 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CAD B 950 |
Chain | Residue |
B | TYR83 |
B | TRP324 |
B | CYS384 |
site_id | BC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE H4B B 600 |
Chain | Residue |
A | TRP447 |
A | PHE462 |
A | HIS463 |
B | SER104 |
B | ARG367 |
B | ALA448 |
B | TRP449 |
B | HEM500 |
B | HOH1247 |
B | HOH1250 |
B | HOH1253 |
B | HOH1301 |
B | HOH1375 |
site_id | BC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE XFJ B 800 |
Chain | Residue |
A | TRP76 |
B | LEU107 |
B | ARG185 |
B | GLN249 |
B | VAL338 |
B | PHE355 |
B | TRP358 |
B | GLU363 |
B | TYR477 |
B | HEM500 |
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 | SER104 | |
B | SER104 | |
B | GLN249 | |
B | TRP358 | |
B | TYR359 | |
B | GLU363 | |
B | ALA448 | |
B | TRP449 | |
B | PHE462 | |
B | TYR477 | |
A | GLN249 | |
A | TRP358 | |
A | TYR359 | |
A | GLU363 | |
A | ALA448 | |
A | TRP449 | |
A | PHE462 | |
A | TYR477 | |
Chain | Residue | Details |
A | CYS186 | |
B | CYS186 | |
Chain | Residue | Details |
A | THR46 | |
B | THR46 | |