Research workbench
AlphaFold monomer V2.0 prediction for 3-methyl-2-oxobutanoate hydroxymethyltransferase (A9MPM1)
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
- A9MPM1
- Type
- protein
- Length
- 263 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4cAEB4755744576CC7C74cfdE50cE222de773212
- Molecule
- 3-methyl-2-oxobutanoate hydroxymethyltransferase
- UniProt
- A9MPM1
- Pockets
- 3 · best druggability 0.67
Structure
1 distinct chain · 45% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3-methyl-2-oxobutanoate hydroxymethyltransferase | protein | 263 | 45% helix, 13% strand | A9MPM1 |
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 | 203 | 0.67 | 0.85 | 31 | empty |
| 2 | 113 | 0.42 | 0.76 | 23 | empty |
| 3 | 70 | 0.38 | 0.78 | 14 | 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 A9MPM1
- Elsewhere: UniProt A9MPM1 · AlphaFold DB A9MPM1
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