Research workbench
Structure of human endothelial nitric oxide synthase heme domain in complex with (R)-3-[(2-amino-4-methylquinolin-7-YL)METHOXY]-5-(2- (METHYLAMINO)PROPYL)BENZONITRILE
Analyse Structure of human endothelial nitric oxide synthase heme domain in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5UOB
- Type
- protein
- Length
- 1,609 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nitric oxide synthase, endothelial
- EC
- 1.14.13.39
- UniProt
- P29474
- Ligands
- M4R, HEM, ZN, GD, CL
- Pockets
- 20 · best druggability 0.85
Structure
x-ray diffraction · 3 distinct chains · 39% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nitric oxide synthase, endothelial (EC 1.14.13.39) | protein | 404 | 39% helix, 16% strand | P29474 |
| B, D | Nitric oxide synthase, endothelial (EC 1.14.13.39) | protein | 402 | 39% helix, 16% strand | P29474 |
| C | Nitric oxide synthase, endothelial (EC 1.14.13.39) | protein | 401 | 39% helix, 15% strand | P29474 |
Ligands and binding sites
- M4R · 3-[(2-amino-4-methylquinolin-7-yl)methoxy]-5-[(2R)-2-(methylamino)propyl]benzonitrile · ligand · 8 copies · chains A, B, C, D
- HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A, B, C, D
- ZN · Zinc ion · metal · 6 copies · chains A, B, C, D
- GD · Gadolinium atom · metal · 4 copies · chains A, B, C, D
- CL · Chloride ion · ion · 4 copies · chains A, B, C, D
- BTB · 2-[bis-(2-hydroxy-ethyl)-amino]-2-hydroxymethyl-propane-1,3-diol · additive · 11 copies · chains A, B, C, D
- GOL · Glycerol · additive · 2 copies · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1000 | 0.85 | 0.86 | 112 | HEM, M4R, CL |
| 2 | 1138 | 0.83 | 0.84 | 99 | HEM, M4R, ZN, CL |
| 3 | 1190 | 0.83 | 0.84 | 94 | HEM, M4R, ZN |
| 4 | 1140 | 0.82 | 0.83 | 87 | ZN, HEM, M4R, CL |
| 5 | 80 | 0.72 | 0.96 | 22 | empty |
Interfaces
4 interfaces between chains.
- C–D · 2602 Ų buried · 43 hydrogen bonds · protein-protein
- A–B · 2599 Ų buried · 42 hydrogen bonds · protein-protein
- B–C · 446 Ų buried · 1 hydrogen bond · protein-protein
- A–C · 66 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 5UOB · Structure of human endothelial nitric oxide synthase heme domain in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P29474
- Elsewhere: RCSB PDB 5UOB · PDBe 5UOB · UniProt P29474
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