Research workbench
AlphaFold monomer V2.0 prediction for 3-methyl-2-oxobutanoate hydroxymethyltransferase (Q215V6)
Analyse AlphaFold monomer V2.0 prediction for 3-methyl-2-oxobutanoate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q215V6
- Type
- protein
- Length
- 274 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB6926Ea66Df63FD8A4A5a32f9B661E4DE7e55427
- Molecule
- 3-methyl-2-oxobutanoate hydroxymethyltransferase
- UniProt
- Q215V6
- Pockets
- 2 · best druggability 0.67
Structure
1 distinct chain · 42% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3-methyl-2-oxobutanoate hydroxymethyltransferase | protein | 274 | 42% helix, 15% strand | Q215V6 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 230 | 0.67 | 0.84 | 33 | empty |
| 2 | 55 | 0.28 | 0.75 | 16 | 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 Q215V6
- Elsewhere: UniProt Q215V6 · AlphaFold DB Q215V6
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