Research workbench
AlphaFold monomer V2.0 prediction for D-serine dehydratase (B5EY75)
Analyse AlphaFold monomer V2.0 prediction for D-serine dehydratase (B5EY75) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B5EY75
- Type
- protein
- Length
- 440 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd6ce0c7C49c82dFd45bc32bF85412d99a1588283
- Molecule
- D-serine dehydratase
- UniProt
- B5EY75
- Pockets
- 2 · best druggability 0.75
Structure
1 distinct chain · 54% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | D-serine dehydratase | protein | 440 | 54% helix, 14% strand | B5EY75 |
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 | 100 | 0.75 | 0.96 | 30 | empty |
| 2 | 196 | 0.49 | 0.76 | 26 | 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 B5EY75
- Elsewhere: UniProt B5EY75 · AlphaFold DB B5EY75
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