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 | TRP178 |
| A | TRP447 |
| A | PHE473 |
| A | TYR475 |
| A | KMM502 |
| A | HOH602 |
| A | HOH678 |
| A | ARG183 |
| A | CYS184 |
| A | SER226 |
| A | PHE353 |
| A | SER354 |
| A | TRP356 |
| A | MET358 |
| A | GLU361 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue KMM A 502 |
| Chain | Residue |
| A | PHE105 |
| A | GLN247 |
| A | VAL336 |
| A | TRP356 |
| A | TYR357 |
| A | GLU361 |
| A | TRP447 |
| A | HEM501 |
| A | KMM503 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue KMM A 503 |
| Chain | Residue |
| A | VAL104 |
| A | ARG365 |
| A | HIS371 |
| A | ALA446 |
| A | TRP447 |
| A | KMM502 |
| B | TRP74 |
| B | PHE460 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue BTB A 504 |
| Chain | Residue |
| A | ASP384 |
| A | GD509 |
| A | HOH607 |
| A | HOH679 |
| B | ASP378 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue BTB A 505 |
| Chain | Residue |
| A | GLU377 |
| A | THR387 |
| B | ASP384 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | binding site for residue BTB A 506 |
| Chain | Residue |
| A | GLU167 |
| B | PRO479 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue BTB A 507 |
| Chain | Residue |
| A | GLU298 |
| B | GLN89 |
| B | SER125 |
| B | ASP129 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 508 |
| Chain | Residue |
| A | CYS94 |
| A | CYS99 |
| B | CYS94 |
| B | CYS99 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue GD A 509 |
| Chain | Residue |
| A | BTB504 |
| A | HOH607 |
| A | HOH679 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue GD A 510 |
| Chain | Residue |
| A | GLU156 |
| A | GLN164 |
| A | HOH661 |
| A | HOH696 |
| B | GLU147 |
| B | HOH659 |
| site_id | AD2 |
| Number of Residues | 14 |
| Details | binding site for residue HEM B 501 |
| Chain | Residue |
| B | TRP178 |
| B | CYS184 |
| B | SER226 |
| B | PHE353 |
| B | SER354 |
| B | TRP356 |
| B | MET358 |
| B | GLU361 |
| B | ARG365 |
| B | TRP447 |
| B | PHE473 |
| B | TYR475 |
| B | KMM502 |
| B | HOH613 |
| site_id | AD3 |
| Number of Residues | 10 |
| Details | binding site for residue KMM B 502 |
| Chain | Residue |
| B | PHE105 |
| B | GLN247 |
| B | PHE353 |
| B | TRP356 |
| B | TYR357 |
| B | GLU361 |
| B | ARG365 |
| B | TRP447 |
| B | TYR475 |
| B | HEM501 |
| site_id | AD4 |
| Number of Residues | 9 |
| Details | binding site for residue KMM B 503 |
| Chain | Residue |
| A | TRP74 |
| A | TRP445 |
| A | PHE460 |
| A | HIS461 |
| B | VAL104 |
| B | ARG365 |
| B | HIS371 |
| B | ALA446 |
| B | TRP447 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue BTB B 504 |
| Chain | Residue |
| A | ASP378 |
| B | THR319 |
| B | GLU321 |
| B | GD507 |
| B | HOH601 |
| B | HOH683 |
| site_id | AD6 |
| Number of Residues | 8 |
| Details | binding site for residue BTB B 505 |
| Chain | Residue |
| B | ASP297 |
| B | GLU298 |
| B | GD508 |
| B | HOH602 |
| B | HOH604 |
| B | HOH643 |
| B | HOH656 |
| B | GLU167 |
| site_id | AD7 |
| Number of Residues | 2 |
| Details | binding site for residue BTB B 506 |
| Chain | Residue |
| A | ARG255 |
| B | GLU377 |
| site_id | AD8 |
| Number of Residues | 6 |
| Details | binding site for residue GD B 507 |
| Chain | Residue |
| A | HOH606 |
| B | THR319 |
| B | GLU321 |
| B | BTB504 |
| B | HOH601 |
| B | HOH683 |
| site_id | AD9 |
| Number of Residues | 5 |
| Details | binding site for residue GD B 508 |
| Chain | Residue |
| B | GLU167 |
| B | BTB505 |
| B | HOH643 |
| B | HOH656 |
| B | HOH736 |
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 | CYS94 | |
| A | CYS99 | |
| B | CYS94 | |
| B | CYS99 | |
| Chain | Residue | Details |
| A | SER102 | |
| A | TYR475 | |
| B | SER102 | |
| B | GLN247 | |
| B | TRP356 | |
| B | TYR357 | |
| B | GLU361 | |
| B | ASN366 | |
| B | ALA446 | |
| B | TRP447 | |
| B | PHE460 | |
| A | GLN247 | |
| B | TYR475 | |
| A | TRP356 | |
| A | TYR357 | |
| A | GLU361 | |
| A | ASN366 | |
| A | ALA446 | |
| A | TRP447 | |
| A | PHE460 | |
| Chain | Residue | Details |
| A | CYS184 | |
| B | CYS184 | |
| Chain | Residue | Details |
| A | ARG365 | |
| B | ARG365 | |
| Chain | Residue | Details |
| A | SER114 | |
| B | SER114 | |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 935 |
| Chain | Residue | Details |
| A | CYS184 | metal ligand |
| A | ARG187 | steric role |
| A | TRP356 | electrostatic stabiliser |
| A | GLU361 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 935 |
| Chain | Residue | Details |
| B | CYS184 | metal ligand |
| B | ARG187 | steric role |
| B | TRP356 | electrostatic stabiliser |
| B | GLU361 | electrostatic stabiliser |
