MolNFT v1 · #158000 · protein
Structure of human endothelial nitric oxide synthase heme domain in complex with 6-(3-fluoro-5-(3-(METHYLAMINO)PROP-1-yn-1-YL)PHENETHYL)- 4-methylpyridin-2-amine
6NH1 · Endothelial nitric oxide synthase splice variant ENOS13A: “Structure of human endothelial nitric oxide synthase heme domain in complex with…”. X-ray diffraction, 6 ligands (HEM, KLY, H4B), 20 pockets (best druggability 0.85). MolNFT…
- PDB
- 6NH1
- Type
- protein
- Length
- 1,614 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endothelial nitric oxide synthase splice variant ENOS13A
- UniProt
- A0S0A6
- Ligands
- HEM, KLY, H4B, 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 | Endothelial nitric oxide synthase splice variant ENOS13A | protein | 404 | 37% helix, 15% strand | A0S0A6 |
| B, D | Endothelial nitric oxide synthase splice variant ENOS13A | protein | 404 | 39% helix, 15% strand | A0S0A6 |
| C | Endothelial nitric oxide synthase splice variant ENOS13A | protein | 402 | 40% helix, 16% strand | A0S0A6 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A, B, C, D
- KLY · 6-(2-{3-fluoro-5-[3-(methylamino)prop-1-yn-1-yl]phenyl}ethyl)-4-methylpyridin-2-amine · ligand · 4 copies · chains A, B, C, D
- H4B · 5,6,7,8-tetrahydrobiopterin · ligand · 4 copies · chains A, B, C, D
- ZN · Zinc ion · metal · 4 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, C, B, 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, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 958 | 0.85 | 0.86 | 86 | HEM, H4B, KLY, ZN |
| 2 | 1068 | 0.85 | 0.86 | 92 | HEM, KLY, CL, H4B |
| 3 | 1086 | 0.85 | 0.85 | 91 | HEM, H4B, KLY, CL, ZN |
| 4 | 1185 | 0.83 | 0.84 | 88 | HEM, H4B, KLY, CL |
| 5 | 86 | 0.72 | 0.95 | 22 | empty |
Interfaces
4 interfaces between chains.
- A–B · 2790 Ų buried · 37 hydrogen bonds · protein-protein
- C–D · 2740 Ų buried · 43 hydrogen bonds · protein-protein
- B–C · 514 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 79 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6NH1 · 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 A0S0A6
- Elsewhere: RCSB PDB 6NH1 · PDBe 6NH1 · UniProt A0S0A6
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