Research workbench
AlphaFold monomer V2.0 prediction for ATP-dependent bile acid permease (P32386)
Analyse AlphaFold monomer V2.0 prediction for ATP-dependent bile acid permease (P32386) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P32386
- Type
- protein
- Length
- 1,661 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8fCa577425962E967D175b7cf864132866e2F7F9
- Molecule
- ATP-dependent bile acid permease
- UniProt
- P32386
- Pockets
- 20 · best druggability 0.84
Structure
1 distinct chain · 62% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent bile acid permease | protein | 1661 | 62% helix, 9% strand | P32386 |
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1039 | 0.84 | 0.85 | 93 | empty |
| 2 | 530 | 0.69 | 0.79 | 47 | empty |
| 3 | 544 | 0.68 | 0.78 | 52 | empty |
| 4 | 71 | 0.66 | 0.93 | 21 | empty |
| 5 | 462 | 0.65 | 0.77 | 59 | empty |
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 P32386
- Elsewhere: UniProt P32386 · AlphaFold DB P32386
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