Research workbench
AlphaFold monomer V2.0 prediction for erythronate-4-phosphate dehydrogenase (A9KTV0)
Analyse AlphaFold monomer V2.0 prediction for erythronate-4-phosphate dehydrogenase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A9KTV0
- Type
- protein
- Length
- 376 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6Ed09D80e98fE15DE51C9E7a8896AbF1f2365C3e
- Molecule
- Erythronate-4-phosphate dehydrogenase
- UniProt
- A9KTV0
- Pockets
- 3 · best druggability 0.68
Structure
1 distinct chain · 39% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Erythronate-4-phosphate dehydrogenase | protein | 376 | 39% helix, 16% strand | A9KTV0 |
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 | 596 | 0.68 | 0.77 | 66 | empty |
| 2 | 69 | 0.32 | 0.75 | 17 | empty |
| 3 | 51 | 0.27 | 0.75 | 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 A9KTV0
- Elsewhere: UniProt A9KTV0 · AlphaFold DB A9KTV0
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