Research workbench
AlphaFold monomer V2.0 prediction for erythronate-4-phosphate dehydrogenase (C1DM66)
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
- C1DM66
- Type
- protein
- Length
- 380 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7dcbAD470f5929B90D67D043964f6a19Cd5f2dD5
- Molecule
- Erythronate-4-phosphate dehydrogenase
- UniProt
- C1DM66
- Pockets
- 3 · best druggability 0.71
Structure
1 distinct chain · 43% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Erythronate-4-phosphate dehydrogenase | protein | 380 | 43% helix, 16% strand | C1DM66 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 639 | 0.71 | 0.78 | 67 | empty |
| 2 | 185 | 0.50 | 0.77 | 29 | empty |
| 3 | 84 | 0.35 | 0.75 | 21 | 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 C1DM66
- Elsewhere: UniProt C1DM66 · AlphaFold DB C1DM66
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