Research workbench
AlphaFold monomer V2.0 prediction for erythronate-4-phosphate dehydrogenase (Q5E452)
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
- Q5E452
- Type
- protein
- Length
- 376 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4Ef77Afb5a3D9F41c95Be3227D1CC986CCb61835
- Molecule
- Erythronate-4-phosphate dehydrogenase
- UniProt
- Q5E452
- Pockets
- 2 · best druggability 0.75
Structure
1 distinct chain · 38% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Erythronate-4-phosphate dehydrogenase | protein | 376 | 38% helix, 16% strand | Q5E452 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 764 | 0.75 | 0.80 | 75 | empty |
| 2 | 61 | 0.30 | 0.75 | 13 | 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 Q5E452
- Elsewhere: UniProt Q5E452 · AlphaFold DB Q5E452
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