MolNFT v1 · #145910 · protein
Crystal structure of an apo chimeric human ALPHA1GABAA receptor
6D1S · Chimeric ALPHA1GABAA receptor: “Crystal structure of an apo chimeric human ALPHA1GABAA receptor”. X-ray diffraction, 20 pockets (best druggability 0.79). MolNFT v1 #145910 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 6D1S
- Type
- protein
- Length
- 3,140 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chimeric ALPHA1GABAA receptor
- UniProt
- E0SJQ4, P14867
- Pockets
- 20 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J | Chimeric ALPHA1GABAA receptor | protein | 314 | 32% helix, 32% strand | E0SJQ4, P14867 |
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 | 1002 | 0.79 | 0.81 | 103 | empty |
| 2 | 931 | 0.79 | 0.81 | 103 | empty |
| 3 | 615 | 0.74 | 0.81 | 77 | empty |
| 4 | 665 | 0.74 | 0.80 | 64 | empty |
| 5 | 1114 | 0.74 | 0.77 | 96 | empty |
Interfaces
11 interfaces between chains.
- H–I · 2668 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 2584 Ų buried · 22 hydrogen bonds · protein-protein
- F–J · 2513 Ų buried · 21 hydrogen bonds · protein-protein
- A–E · 2502 Ų buried · 17 hydrogen bonds · protein-protein
- C–D · 2500 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 6D1S · Crystal structure of an apo chimeric human alpha1GABAA receptor · the same entry in another collection · chain J against J, TM-score 1.00
- P14867 · AlphaFold monomer V2.0 prediction for gamma-aminobutyric acid receptor subunit alpha-1… · a predicted model of the same protein · chain H against A, TM-score 0.90
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
- Every structure of UniProt P14867
- Elsewhere: RCSB PDB 6D1S · PDBe 6D1S · UniProt E0SJQ4 · UniProt P14867
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