Research workbench
AlphaFold monomer V2.0 prediction for thiamine-phosphate synthase (A5VKA1)
Analyse AlphaFold monomer V2.0 prediction for thiamine-phosphate synthase (A5VKA1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5VKA1
- Type
- protein
- Length
- 215 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBe5052869ae2CCfE8B362617F53C763F9782C97e
- Molecule
- Thiamine-phosphate synthase
- UniProt
- A5VKA1
- Pockets
- 1 · best druggability 0.71
Structure
1 distinct chain · 43% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thiamine-phosphate synthase | protein | 215 | 43% helix, 16% strand | A5VKA1 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 232 | 0.71 | 0.87 | 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 A5VKA1
- Elsewhere: UniProt A5VKA1 · AlphaFold DB A5VKA1
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