Research workbench
AlphaFold monomer V2.0 prediction for 3-methyl-2-oxobutanoate hydroxymethyltransferase (Q16DW5)
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
- Q16DW5
- Type
- protein
- Length
- 279 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7782F4817b37743d738e9aF842bf74bd50f2015E
- Molecule
- 3-methyl-2-oxobutanoate hydroxymethyltransferase
- UniProt
- Q16DW5
- Pockets
- 3 · best druggability 0.72
Structure
1 distinct chain · 41% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3-methyl-2-oxobutanoate hydroxymethyltransferase | protein | 279 | 41% helix, 14% strand | Q16DW5 |
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 | 240 | 0.72 | 0.86 | 30 | empty |
| 2 | 90 | 0.37 | 0.76 | 17 | empty |
| 3 | 66 | 0.33 | 0.76 | 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 Q16DW5
- Elsewhere: UniProt Q16DW5 · AlphaFold DB Q16DW5
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