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 |
A | 0020037 | molecular_function | heme binding |
B | 0004517 | molecular_function | nitric-oxide synthase activity |
B | 0006809 | biological_process | nitric oxide biosynthetic process |
B | 0020037 | molecular_function | heme binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACT A 860 |
Chain | Residue |
A | GLY188 |
A | TRP358 |
A | VAL420 |
A | SER428 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT B 861 |
Chain | Residue |
B | TRP358 |
B | SER428 |
B | ACT862 |
B | HOH1043 |
B | HOH1173 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ACT B 862 |
Chain | Residue |
B | ACT861 |
B | HOH1043 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 900 |
Chain | Residue |
A | CYS96 |
A | CYS101 |
B | CYS96 |
B | CYS101 |
site_id | AC5 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE HEM A 700 |
Chain | Residue |
A | TRP180 |
A | ARG185 |
A | CYS186 |
A | SER228 |
A | PHE355 |
A | SER356 |
A | TRP358 |
A | GLU363 |
A | TRP449 |
A | TYR477 |
A | H4B760 |
A | DP9799 |
A | HOH963 |
A | HOH975 |
A | HOH980 |
A | HOH997 |
site_id | AC6 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE H4B A 760 |
Chain | Residue |
A | SER104 |
A | ARG367 |
A | ALA448 |
A | TRP449 |
A | HEM700 |
A | GOL880 |
A | HOH902 |
A | HOH963 |
A | HOH968 |
B | TRP447 |
B | PHE462 |
B | HIS463 |
B | GLN464 |
B | GLU465 |
B | HOH968 |
site_id | AC7 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE DP9 A 799 |
Chain | Residue |
A | GLN249 |
A | PRO336 |
A | VAL338 |
A | SER356 |
A | GLY357 |
A | TRP358 |
A | GLU363 |
A | TYR477 |
A | HEM700 |
A | HOH963 |
A | HOH997 |
A | HOH1001 |
A | HOH1087 |
A | HOH1112 |
A | HOH1157 |
site_id | AC8 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE HEM B 700 |
Chain | Residue |
B | TRP180 |
B | ARG185 |
B | CYS186 |
B | SER228 |
B | PHE355 |
B | SER356 |
B | TRP358 |
B | GLU363 |
B | TRP449 |
B | TYR477 |
B | H4B761 |
B | DP9800 |
B | HOH904 |
B | HOH921 |
B | HOH923 |
B | HOH940 |
site_id | AC9 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE H4B B 761 |
Chain | Residue |
A | TRP447 |
A | PHE462 |
A | HIS463 |
A | GLU465 |
B | SER104 |
B | ARG367 |
B | ALA448 |
B | TRP449 |
B | HEM700 |
B | GOL881 |
B | HOH886 |
B | HOH921 |
B | HOH933 |
B | HOH1011 |
site_id | BC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE DP9 B 800 |
Chain | Residue |
B | TYR477 |
B | HEM700 |
B | GOL881 |
B | HOH921 |
B | HOH940 |
B | HOH1001 |
B | HOH1019 |
B | HOH1072 |
B | GLN249 |
B | PRO336 |
B | VAL338 |
B | SER356 |
B | GLY357 |
B | TRP358 |
B | GLU363 |
B | TRP449 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 880 |
Chain | Residue |
A | VAL106 |
A | ARG367 |
A | HIS373 |
A | H4B760 |
B | HOH968 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 881 |
Chain | Residue |
B | VAL106 |
B | ARG367 |
B | HIS373 |
B | H4B761 |
B | DP9800 |
B | HOH1011 |
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 | THR97 | |
A | LEU102 | |
B | THR97 | |
B | LEU102 | |
Chain | Residue | Details |
A | LEU105 | |
A | GLN478 | |
B | LEU105 | |
B | LEU250 | |
B | TYR359 | |
B | MET360 | |
B | ILE364 | |
B | LEU369 | |
B | TRP449 | |
B | ILE450 | |
B | HIS463 | |
A | LEU250 | |
B | GLN478 | |
A | TYR359 | |
A | MET360 | |
A | ILE364 | |
A | LEU369 | |
A | TRP449 | |
A | ILE450 | |
A | HIS463 | |
Chain | Residue | Details |
A | VAL187 | |
B | VAL187 | |
Chain | Residue | Details |
A | PRO117 | |
B | PRO117 | |