Research workbench
AlphaFold monomer V2.0 prediction for 3-methyl-2-oxobutanoate hydroxymethyltransferase (Q21F95)
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
- Q21F95
- Type
- protein
- Length
- 270 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xF8cD1d8d93E9783063700De244A6e3cf6A195579
- Molecule
- 3-methyl-2-oxobutanoate hydroxymethyltransferase
- UniProt
- Q21F95
- Pockets
- 3 · best druggability 0.70
Structure
1 distinct chain · 44% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3-methyl-2-oxobutanoate hydroxymethyltransferase | protein | 270 | 44% helix, 14% strand | Q21F95 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 236 | 0.70 | 0.85 | 33 | empty |
| 2 | 115 | 0.43 | 0.77 | 22 | empty |
| 3 | 91 | 0.34 | 0.74 | 21 | 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 Q21F95
- Elsewhere: UniProt Q21F95 · AlphaFold DB Q21F95
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