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 |