Research workbench
AlphaFold monomer V2.0 prediction for probable D-serine dehydratase (A0RCF8)
Analyse AlphaFold monomer V2.0 prediction for probable D-serine dehydratase (A0RCF8) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A0RCF8
- Type
- protein
- Length
- 446 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xfdf43E25548A6F2259b983138c11e47b2f207335
- Molecule
- Probable D-serine dehydratase
- UniProt
- A0RCF8
- Pockets
- 4 · best druggability 0.72
Structure
1 distinct chain · 53% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Probable D-serine dehydratase | protein | 446 | 53% helix, 12% strand | A0RCF8 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 56 | 0.72 | 0.98 | 27 | empty |
| 2 | 62 | 0.40 | 0.81 | 16 | empty |
| 3 | 53 | 0.34 | 0.78 | 12 | empty |
| 4 | 67 | 0.32 | 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 A0RCF8
- Elsewhere: UniProt A0RCF8 · AlphaFold DB A0RCF8
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