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 ZN A 903 |
| Chain | Residue |
| A | CYS94 |
| A | CYS99 |
| B | CYS94 |
| B | CYS99 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HEM A 901 |
| Chain | Residue |
| A | TRP356 |
| A | GLU361 |
| A | TRP447 |
| A | TYR475 |
| A | 7NI906 |
| A | HOH937 |
| A | HOH1104 |
| A | TRP178 |
| A | ARG183 |
| A | CYS184 |
| A | PHE353 |
| A | SER354 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE HEM B 901 |
| Chain | Residue |
| B | TRP178 |
| B | ARG183 |
| B | CYS184 |
| B | PHE353 |
| B | SER354 |
| B | TRP356 |
| B | MET358 |
| B | GLU361 |
| B | TRP447 |
| B | PHE473 |
| B | TYR475 |
| B | 7NI907 |
| B | HOH995 |
| B | HOH1072 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE 7NI A 906 |
| Chain | Residue |
| A | PRO334 |
| A | VAL336 |
| A | GLY355 |
| A | TRP356 |
| A | TYR357 |
| A | MET358 |
| A | GLU361 |
| A | HEM901 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE 7NI B 907 |
| Chain | Residue |
| B | PRO334 |
| B | VAL336 |
| B | GLY355 |
| B | TRP356 |
| B | TYR357 |
| B | MET358 |
| B | GLU361 |
| B | HEM901 |
Functional Information from PROSITE/UniProt
| site_id | PS60001 |
| Number of Residues | 8 |
| Details | NOS Nitric oxide synthase (NOS) signature. RCVGRIqW |
| Chain | Residue | Details |
| A | ARG183-TRP190 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10074942, ECO:0000269|PubMed:12437348, ECO:0000269|PubMed:18849972, ECO:0000269|PubMed:25286850, ECO:0007744|PDB:1M9J, ECO:0007744|PDB:1M9K, ECO:0007744|PDB:1M9M, ECO:0007744|PDB:1M9Q, ECO:0007744|PDB:1M9R, ECO:0007744|PDB:3EAH, ECO:0007744|PDB:3NOS, ECO:0007744|PDB:4D1O, ECO:0007744|PDB:4D1P |
| Chain | Residue | Details |
| A | THR95 | |
| A | LEU100 | |
| B | THR95 | |
| B | LEU100 | |
| Chain | Residue | Details |
| A | LEU103 | |
| A | GLN476 | |
| B | LEU103 | |
| B | LEU248 | |
| B | TYR357 | |
| B | MET358 | |
| B | ILE362 | |
| B | LEU367 | |
| B | TRP447 | |
| B | ILE448 | |
| B | HIS461 | |
| A | LEU248 | |
| B | GLN476 | |
| A | TYR357 | |
| A | MET358 | |
| A | ILE362 | |
| A | LEU367 | |
| A | TRP447 | |
| A | ILE448 | |
| A | HIS461 | |
| Chain | Residue | Details |
| A | VAL185 | |
| B | VAL185 | |
| Chain | Residue | Details |
| A | ASN366 | |
| B | ASN366 | |
| Chain | Residue | Details |
| A | PRO115 | |
| B | PRO115 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 3nos |
| Chain | Residue | Details |
| A | TRP356 | |
| A | ARG187 | |
| A | GLU361 | |
| A | CYS184 | |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 3nos |
| Chain | Residue | Details |
| B | TRP356 | |
| B | ARG187 | |
| B | GLU361 | |
| B | CYS184 | |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 935 |
| Chain | Residue | Details |
| A | VAL185 | metal ligand |
| A | ILE188 | steric role |
| A | TYR357 | electrostatic stabiliser |
| A | ILE362 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 935 |
| Chain | Residue | Details |
| B | VAL185 | metal ligand |
| B | ILE188 | steric role |
| B | TYR357 | electrostatic stabiliser |
| B | ILE362 | electrostatic stabiliser |
