MolNFT v1 · #81424 · protein
X-ray structure of a pentameric ligand gated ion channel from erwinia chrysanthemi (elic) mutant L240S F247L (L9S F16L) in presence of 10 mm cysteamine
3UQ7 · Gamma-aminobutyric-acid receptor subunit beta-1: “X-ray structure of a pentameric ligand gated ion channel from erwinia chrysanthemi (elic) mutant L240S F247L…”. X-ray diffraction, 20 pockets (best druggability 0.82). MolNFT v1…
- PDB
- 3UQ7
- Type
- protein
- Length
- 3,070 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gamma-aminobutyric-acid receptor subunit beta-1
- UniProt
- E0SJQ4
- Pockets
- 20 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J | Gamma-aminobutyric-acid receptor subunit beta-1 | protein | 307 | 28% helix, 32% strand | E0SJQ4 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 678 | 0.82 | 0.86 | 55 | empty |
| 2 | 678 | 0.82 | 0.86 | 75 | empty |
| 3 | 756 | 0.81 | 0.85 | 77 | empty |
| 4 | 720 | 0.81 | 0.85 | 83 | empty |
| 5 | 670 | 0.81 | 0.86 | 55 | empty |
Interfaces
18 interfaces between chains.
- H–I · 2697 Ų buried · 22 hydrogen bonds · protein-protein
- G–H · 2696 Ų buried · 21 hydrogen bonds · protein-protein
- B–C · 2694 Ų buried · 22 hydrogen bonds · protein-protein
- F–G · 2685 Ų buried · 21 hydrogen bonds · protein-protein
- C–D · 2683 Ų buried · 22 hydrogen bonds · protein-protein
Compared structures
- 3UQ7 · X-ray structure of a pentameric ligand gated ion channel from Erwinia chrysanthemi (ELIC)… · 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 E0SJQ4
- Elsewhere: RCSB PDB 3UQ7 · PDBe 3UQ7 · UniProt E0SJQ4
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