MolNFT v1 · #158002 · protein
Structure of human endothelial nitric oxide synthase heme domain in complex with (S)-6-(3-fluoro-5-(2-(pyrrolidin-2-YL)ETHYL)PHENETHYL)- 4-methylpyridin-2-amine
6NH3 · Endothelial nitric oxide synthase splice variant ENOS13A: “Structure of human endothelial nitric oxide synthase heme domain in complex with…”. X-ray diffraction, 5 ligands (KL4, HEM, ZN), 20 pockets (best druggability 0.85). MolNFT…
- PDB
- 6NH3
- Type
- protein
- Length
- 1,609 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
- KL4, 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 | Endothelial nitric oxide synthase splice variant ENOS13A | protein | 404 | 38% helix, 15% strand | A0S0A6 |
| B, D | Endothelial nitric oxide synthase splice variant ENOS13A | protein | 402 | 40% helix, 14% strand | A0S0A6 |
| C | Endothelial nitric oxide synthase splice variant ENOS13A | protein | 401 | 38% helix, 15% strand | A0S0A6 |
Ligands and binding sites
- KL4 · 6-[2-(3-fluoro-5-{2-[(2S)-pyrrolidin-2-yl]ethyl}phenyl)ethyl]-4-methylpyridin-2-amine · 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, C, B, 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 · 9 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, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1082 | 0.85 | 0.86 | 97 | HEM, KL4, CL, ZN |
| 2 | 1190 | 0.84 | 0.85 | 94 | HEM, KL4, CL, ZN |
| 3 | 1133 | 0.84 | 0.84 | 92 | KL4, ZN, HEM, CL |
| 4 | 1146 | 0.83 | 0.84 | 91 | KL4, ZN, HEM, CL |
| 5 | 99 | 0.73 | 0.95 | 22 | empty |
Interfaces
4 interfaces between chains.
- A–B · 2740 Ų buried · 43 hydrogen bonds · protein-protein
- C–D · 2602 Ų buried · 37 hydrogen bonds · protein-protein
- B–C · 489 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 129 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 6NH3 · 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 6NH3 · PDBe 6NH3 · UniProt A0S0A6
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