Research workbench
AlphaFold monomer V2.0 prediction for 3-methyl-2-oxobutanoate hydroxymethyltransferase (Q326A3)
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
- Q326A3
- Type
- protein
- Length
- 264 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb3c0C983Fc44934AC589D7131C08a72544EBB92E
- Molecule
- 3-methyl-2-oxobutanoate hydroxymethyltransferase
- UniProt
- Q326A3
- Pockets
- 3 · best druggability 0.65
Structure
1 distinct chain · 45% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3-methyl-2-oxobutanoate hydroxymethyltransferase | protein | 264 | 45% helix, 14% strand | Q326A3 |
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 | 229 | 0.65 | 0.83 | 32 | empty |
| 2 | 104 | 0.41 | 0.77 | 17 | empty |
| 3 | 106 | 0.38 | 0.75 | 22 | 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 Q326A3
- Elsewhere: UniProt Q326A3 · AlphaFold DB Q326A3
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