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 | SER428 |
A | HEM700 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ACT B 861 |
Chain | Residue |
B | TRP358 |
B | VAL420 |
B | SER428 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 900 |
Chain | Residue |
B | CYS96 |
B | CYS101 |
A | CYS96 |
A | CYS101 |
site_id | AC4 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE HEM A 700 |
Chain | Residue |
A | TRP180 |
A | ARG185 |
A | CYS186 |
A | VAL187 |
A | PHE355 |
A | SER356 |
A | TRP358 |
A | GLU363 |
A | TRP449 |
A | PHE475 |
A | TYR477 |
A | H4B760 |
A | DP9799 |
A | ACT860 |
A | HOH913 |
A | HOH957 |
A | HOH964 |
A | HOH1039 |
A | HOH1064 |
site_id | AC5 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE H4B A 760 |
Chain | Residue |
A | SER104 |
A | MET106 |
A | ARG367 |
A | ALA448 |
A | TRP449 |
A | HEM700 |
A | HOH913 |
A | HOH925 |
A | HOH933 |
A | HOH991 |
A | HOH1055 |
B | TRP447 |
B | PHE462 |
B | HIS463 |
B | GLN464 |
B | GLU465 |
site_id | AC6 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE DP9 A 799 |
Chain | Residue |
A | GLN249 |
A | PRO336 |
A | VAL338 |
A | PHE355 |
A | SER356 |
A | GLY357 |
A | TRP358 |
A | GLU363 |
A | TYR477 |
A | HEM700 |
A | HOH913 |
A | HOH1007 |
A | HOH1039 |
A | HOH1056 |
site_id | AC7 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE HEM B 700 |
Chain | Residue |
B | TRP180 |
B | ARG185 |
B | CYS186 |
B | VAL187 |
B | SER228 |
B | PHE355 |
B | SER356 |
B | GLY357 |
B | TRP358 |
B | GLU363 |
B | TRP449 |
B | PHE475 |
B | TYR477 |
B | H4B761 |
B | DP9800 |
B | HOH862 |
B | HOH869 |
B | HOH877 |
B | HOH879 |
B | HOH971 |
site_id | AC8 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE H4B B 761 |
Chain | Residue |
A | TRP447 |
A | PHE462 |
A | HIS463 |
A | GLN464 |
A | GLU465 |
B | SER104 |
B | MET106 |
B | ARG367 |
B | ALA448 |
B | TRP449 |
B | HEM700 |
B | HOH869 |
B | HOH912 |
B | HOH929 |
B | HOH941 |
site_id | AC9 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE DP9 B 800 |
Chain | Residue |
B | GLY357 |
B | TRP358 |
B | GLU363 |
B | TYR477 |
B | HEM700 |
B | HOH862 |
B | HOH869 |
B | HOH894 |
B | HOH898 |
B | HOH1012 |
B | GLN249 |
B | PRO336 |
B | VAL338 |
B | SER356 |
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 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 3nos |
Chain | Residue | Details |
A | CYS186 | |
A | ARG189 | |
A | GLU363 | |
A | TRP358 | |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 3nos |
Chain | Residue | Details |
B | CYS186 | |
B | ARG189 | |
B | GLU363 | |
B | TRP358 | |