Research workbench
AlphaFold monomer V2.0 prediction for thiamine diphosphate dependent-3-acetyloctanal synthase pigd (Q5W251)
Analyse AlphaFold monomer V2.0 prediction for thiamine diphosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5W251
- Type
- protein
- Length
- 904 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBeB220F0B5b0C48F46B5DDd3E3b071BC0827f8D6
- Molecule
- Thiamine diphosphate dependent-3-acetyloctanal synthase pigd
- UniProt
- Q5W251
- Pockets
- 14 · best druggability 0.66
Structure
1 distinct chain · 37% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thiamine diphosphate dependent-3-acetyloctanal synthase pigd | protein | 904 | 37% helix, 19% strand | Q5W251 |
Pockets
14 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 141 | 0.66 | 0.88 | 27 | empty |
| 2 | 310 | 0.63 | 0.80 | 39 | empty |
| 3 | 358 | 0.57 | 0.76 | 42 | empty |
| 4 | 64 | 0.52 | 0.86 | 21 | empty |
| 5 | 141 | 0.50 | 0.79 | 29 | 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 Q5W251
- Elsewhere: UniProt Q5W251 · AlphaFold DB Q5W251
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