Research workbench
AlphaFold monomer V2.0 prediction for erythronate-4-phosphate dehydrogenase (Q1QE21)
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
- Q1QE21
- Type
- protein
- Length
- 386 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x953a45c1afa6C5147a9c9dE66B77afE523F6E050
- Molecule
- Erythronate-4-phosphate dehydrogenase
- UniProt
- Q1QE21
- Pockets
- 3 · best druggability 0.72
Structure
1 distinct chain · 37% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Erythronate-4-phosphate dehydrogenase | protein | 386 | 37% helix, 17% strand | Q1QE21 |
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 | 650 | 0.72 | 0.79 | 67 | empty |
| 2 | 65 | 0.34 | 0.77 | 21 | empty |
| 3 | 59 | 0.29 | 0.74 | 12 | 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 Q1QE21
- Elsewhere: UniProt Q1QE21 · AlphaFold DB Q1QE21
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