Research workbench
AlphaFold monomer V2.0 prediction for erythronate-4-phosphate dehydrogenase (B5FPL4)
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
- B5FPL4
- Type
- protein
- Length
- 378 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1B0853573D9aD0293B54abd19aa139e43c491a8e
- Molecule
- Erythronate-4-phosphate dehydrogenase
- UniProt
- B5FPL4
- Pockets
- 2 · best druggability 0.73
Structure
1 distinct chain · 40% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Erythronate-4-phosphate dehydrogenase | protein | 378 | 40% helix, 17% strand | B5FPL4 |
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 | 709 | 0.73 | 0.79 | 66 | empty |
| 2 | 51 | 0.39 | 0.81 | 11 | 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 B5FPL4
- Elsewhere: UniProt B5FPL4 · AlphaFold DB B5FPL4
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