8UFR
Structure of human endothelial nitric oxide synthase heme domain in complex with 4-methyl-7-(4-methyl-2,3,4,5-tetrahydrobenzo[f][1,4]oxazepin-7-yl)quinolin-2-amine dihydrochloride
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 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 |
site_id | SWS_FT_FI2 |
Number of Residues | 40 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25286850, ECO:0007744|PDB:4D1O |
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 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: axial binding residue => ECO:0000269|PubMed:25286850, ECO:0007744|PDB:4D1O |
Chain | Residue | Details |
A | CYS184 | |
B | CYS184 | |
C | CYS184 | |
D | CYS184 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10074942, ECO:0000269|PubMed:25286850, ECO:0007744|PDB:3NOS, ECO:0007744|PDB:4D1O, ECO:0007744|PDB:4D1P |
Chain | Residue | Details |
A | ARG365 | |
B | ARG365 | |
C | ARG365 | |
D | ARG365 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine; by CDK5 => ECO:0000269|PubMed:20213743 |
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 |