Research workbench
AlphaFold monomer V2.0 prediction for biotin synthase (A7HG97)
Analyse AlphaFold monomer V2.0 prediction for biotin synthase (A7HG97) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A7HG97
- Type
- protein
- Length
- 368 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9F605311B7e26e76340423EfAfbE5e2EFc7A0b7C
- Molecule
- Biotin synthase
- UniProt
- A7HG97
- Pockets
- 2 · best druggability 0.86
Structure
1 distinct chain · 37% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Biotin synthase | protein | 368 | 37% helix, 14% strand | A7HG97 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 588 | 0.86 | 0.92 | 73 | empty |
| 2 | 247 | 0.57 | 0.78 | 38 | 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 A7HG97
- Elsewhere: UniProt A7HG97 · AlphaFold DB A7HG97
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