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 |
C | 0004517 | molecular_function | nitric-oxide synthase activity |
C | 0006809 | biological_process | nitric oxide biosynthetic process |
D | 0004517 | molecular_function | nitric-oxide synthase activity |
D | 0006809 | biological_process | nitric oxide biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | binding site for residue HEM A 501 |
Chain | Residue |
A | TRP178 |
A | MET358 |
A | GLU361 |
A | PHE473 |
A | TYR475 |
A | H4B502 |
A | F2J503 |
A | HOH661 |
A | PRO182 |
A | ARG183 |
A | CYS184 |
A | SER226 |
A | PHE353 |
A | SER354 |
A | GLY355 |
A | TRP356 |
site_id | AC2 |
Number of Residues | 11 |
Details | binding site for residue H4B A 502 |
Chain | Residue |
A | SER102 |
A | ARG365 |
A | ALA446 |
A | TRP447 |
A | HEM501 |
A | HOH628 |
B | TRP445 |
B | PHE460 |
B | GLN462 |
B | GLU463 |
B | HOH609 |
site_id | AC3 |
Number of Residues | 8 |
Details | binding site for residue F2J A 503 |
Chain | Residue |
A | PRO334 |
A | VAL336 |
A | PHE353 |
A | SER354 |
A | GLY355 |
A | TRP356 |
A | GLU361 |
A | HEM501 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue BTB A 504 |
Chain | Residue |
A | CYS382 |
A | ASP384 |
D | BTB506 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue BTB A 505 |
Chain | Residue |
A | GLU377 |
A | HOH608 |
A | HOH651 |
D | ASP384 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue ZN A 506 |
Chain | Residue |
A | CYS94 |
A | CYS99 |
B | CYS94 |
B | CYS99 |
site_id | AC7 |
Number of Residues | 1 |
Details | binding site for residue GOL A 507 |
site_id | AC8 |
Number of Residues | 4 |
Details | binding site for residue CL A 508 |
Chain | Residue |
A | GLN247 |
A | TYR357 |
A | ASN366 |
A | HOH668 |
site_id | AC9 |
Number of Residues | 2 |
Details | binding site for residue GD A 509 |
Chain | Residue |
A | HOH691 |
A | HOH696 |
site_id | AD1 |
Number of Residues | 17 |
Details | binding site for residue HEM B 501 |
Chain | Residue |
B | TRP178 |
B | PRO182 |
B | ARG183 |
B | CYS184 |
B | SER226 |
B | PHE353 |
B | SER354 |
B | TRP356 |
B | GLU361 |
B | TRP447 |
B | PHE473 |
B | TYR475 |
B | H4B502 |
B | F2J503 |
B | HOH610 |
B | HOH629 |
B | HOH682 |
site_id | AD2 |
Number of Residues | 13 |
Details | binding site for residue H4B B 502 |
Chain | Residue |
A | TRP445 |
A | PHE460 |
A | HIS461 |
A | GLN462 |
B | SER102 |
B | VAL104 |
B | ARG365 |
B | ALA446 |
B | TRP447 |
B | HEM501 |
B | HOH610 |
B | HOH616 |
B | HOH674 |
site_id | AD3 |
Number of Residues | 9 |
Details | binding site for residue F2J B 503 |
Chain | Residue |
B | GLN247 |
B | PRO334 |
B | VAL336 |
B | PHE353 |
B | SER354 |
B | GLY355 |
B | TRP356 |
B | GLU361 |
B | HEM501 |
site_id | AD4 |
Number of Residues | 10 |
Details | binding site for residue BTB B 504 |
Chain | Residue |
C | TYR373 |
C | ASN374 |
C | ASP378 |
B | THR319 |
B | GLU321 |
B | GD508 |
B | HOH602 |
B | HOH603 |
C | SER260 |
C | VAL261 |
site_id | AD5 |
Number of Residues | 2 |
Details | binding site for residue BTB B 505 |
Chain | Residue |
B | ASP297 |
B | GLU298 |
site_id | AD6 |
Number of Residues | 2 |
Details | binding site for residue BTB B 506 |
Chain | Residue |
B | ASN374 |
B | ASP378 |
site_id | AD7 |
Number of Residues | 4 |
Details | binding site for residue CL B 507 |
Chain | Residue |
B | GLN247 |
B | TYR357 |
B | ASN366 |
B | HOH686 |
site_id | AD8 |
Number of Residues | 5 |
Details | binding site for residue GD B 508 |
Chain | Residue |
B | THR319 |
B | GLU321 |
B | BTB504 |
B | HOH602 |
C | HOH611 |
site_id | AD9 |
Number of Residues | 15 |
Details | binding site for residue HEM C 501 |
Chain | Residue |
C | TRP178 |
C | ALA181 |
C | PRO182 |
C | ARG183 |
C | CYS184 |
C | SER226 |
C | PHE353 |
C | SER354 |
C | TRP356 |
C | GLU361 |
C | PHE473 |
C | TYR475 |
C | H4B502 |
C | F2J503 |
C | HOH628 |
site_id | AE1 |
Number of Residues | 13 |
Details | binding site for residue H4B C 502 |
Chain | Residue |
C | SER102 |
C | ARG365 |
C | ALA446 |
C | TRP447 |
C | HEM501 |
C | HOH639 |
C | HOH647 |
C | HOH669 |
C | HOH681 |
D | TRP445 |
D | PHE460 |
D | GLN462 |
D | GLU463 |
site_id | AE2 |
Number of Residues | 9 |
Details | binding site for residue F2J C 503 |
Chain | Residue |
C | GLN247 |
C | PRO334 |
C | VAL336 |
C | PHE353 |
C | SER354 |
C | GLY355 |
C | TRP356 |
C | GLU361 |
C | HEM501 |
site_id | AE3 |
Number of Residues | 3 |
Details | binding site for residue BTB C 504 |
Chain | Residue |
C | VAL381 |
C | CYS382 |
C | ASP384 |
site_id | AE4 |
Number of Residues | 2 |
Details | binding site for residue BTB C 505 |
Chain | Residue |
B | ASP384 |
C | GLU377 |
site_id | AE5 |
Number of Residues | 1 |
Details | binding site for residue BTB C 506 |
site_id | AE6 |
Number of Residues | 4 |
Details | binding site for residue ZN C 507 |
Chain | Residue |
C | CYS94 |
C | CYS99 |
D | CYS94 |
D | CYS99 |
site_id | AE7 |
Number of Residues | 2 |
Details | binding site for residue GOL C 508 |
Chain | Residue |
C | GLU167 |
C | HOH618 |
site_id | AE8 |
Number of Residues | 3 |
Details | binding site for residue CL C 509 |
Chain | Residue |
C | GLN247 |
C | TYR357 |
C | ASN366 |
site_id | AE9 |
Number of Residues | 5 |
Details | binding site for residue GD C 510 |
Chain | Residue |
A | GLN257 |
B | HOH761 |
C | ASP384 |
C | HOH690 |
C | HOH710 |
site_id | AF1 |
Number of Residues | 16 |
Details | binding site for residue HEM D 501 |
Chain | Residue |
D | TRP178 |
D | ALA181 |
D | ARG183 |
D | CYS184 |
D | SER226 |
D | PHE353 |
D | SER354 |
D | TRP356 |
D | GLU361 |
D | PHE473 |
D | TYR475 |
D | H4B502 |
D | F2J503 |
D | HOH603 |
D | HOH606 |
D | HOH641 |
site_id | AF2 |
Number of Residues | 11 |
Details | binding site for residue H4B D 502 |
Chain | Residue |
C | TRP445 |
C | PHE460 |
C | GLU463 |
C | HOH640 |
D | SER102 |
D | ARG365 |
D | ALA446 |
D | TRP447 |
D | HEM501 |
D | HOH641 |
D | HOH655 |
site_id | AF3 |
Number of Residues | 9 |
Details | binding site for residue F2J D 503 |
Chain | Residue |
D | GLN247 |
D | PRO334 |
D | VAL336 |
D | PHE353 |
D | GLY355 |
D | TRP356 |
D | GLU361 |
D | HEM501 |
D | HOH667 |
site_id | AF4 |
Number of Residues | 9 |
Details | binding site for residue BTB D 504 |
Chain | Residue |
A | VAL261 |
A | TYR373 |
A | ASN374 |
A | ASP378 |
D | THR319 |
D | GLU321 |
D | GD507 |
D | HOH612 |
D | HOH702 |
site_id | AF5 |
Number of Residues | 3 |
Details | binding site for residue BTB D 505 |
Chain | Residue |
B | GLU167 |
D | GLU298 |
D | HOH642 |
site_id | AF6 |
Number of Residues | 4 |
Details | binding site for residue BTB D 506 |
Chain | Residue |
A | BTB504 |
D | GLU377 |
D | ASP378 |
D | HOH620 |
site_id | AF7 |
Number of Residues | 5 |
Details | binding site for residue GD D 507 |
Chain | Residue |
D | THR319 |
D | GLU321 |
D | BTB504 |
D | HOH698 |
D | HOH702 |
site_id | AF8 |
Number of Residues | 3 |
Details | binding site for residue CL D 508 |
Chain | Residue |
D | GLN247 |
D | TYR357 |
D | ASN366 |
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 | 8 |
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 | |
C | CYS94 | |
C | CYS99 | |
D | CYS94 | |
D | 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 | |
C | SER102 | |
C | GLN247 | |
C | TRP356 | |
C | TYR357 | |
C | GLU361 | |
C | ASN366 | |
C | ALA446 | |
C | TRP447 | |
C | PHE460 | |
A | TRP356 | |
C | TYR475 | |
D | SER102 | |
D | GLN247 | |
D | TRP356 | |
D | TYR357 | |
D | GLU361 | |
D | ASN366 | |
D | ALA446 | |
D | TRP447 | |
D | PHE460 | |
A | TYR357 | |
D | TYR475 | |
A | GLU361 | |
A | ASN366 | |
A | ALA446 | |
A | TRP447 | |
A | PHE460 | |
Chain | Residue | Details |
A | CYS184 | |
B | CYS184 | |
C | CYS184 | |
D | CYS184 | |
Chain | Residue | Details |
A | ARG365 | |
B | ARG365 | |
C | ARG365 | |
D | ARG365 | |
Chain | Residue | Details |
A | SER114 | |
B | SER114 | |
C | SER114 | |
D | 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 |
site_id | MCSA3 |
Number of Residues | 4 |
Details | M-CSA 935 |
Chain | Residue | Details |
C | CYS184 | metal ligand |
C | ARG187 | steric role |
C | TRP356 | electrostatic stabiliser |
C | GLU361 | electrostatic stabiliser |
site_id | MCSA4 |
Number of Residues | 4 |
Details | M-CSA 935 |
Chain | Residue | Details |
D | CYS184 | metal ligand |
D | ARG187 | steric role |
D | TRP356 | electrostatic stabiliser |
D | GLU361 | electrostatic stabiliser |