Research workbench
AlphaFold monomer V2.0 prediction for L-threonine 3-dehydrogenase (Q6MD15)
Analyse AlphaFold monomer V2.0 prediction for L-threonine 3-dehydrogenase (Q6MD15) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q6MD15
- Type
- protein
- Length
- 342 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x865acfe44C28f1b23736f7fd8Da864CcBc33E693
- Molecule
- L-threonine 3-dehydrogenase
- UniProt
- Q6MD15
- Pockets
- 3 · best druggability 0.70
Structure
1 distinct chain · 32% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-threonine 3-dehydrogenase | protein | 342 | 32% helix, 27% strand | Q6MD15 |
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 | 529 | 0.70 | 0.79 | 45 | empty |
| 2 | 66 | 0.33 | 0.76 | 12 | empty |
| 3 | 59 | 0.30 | 0.74 | 18 | 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 Q6MD15
- Elsewhere: UniProt Q6MD15 · AlphaFold DB Q6MD15
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