Research workbench
AlphaFold monomer V2.0 prediction for D-serine dehydratase (A9MWI4)
Analyse AlphaFold monomer V2.0 prediction for D-serine dehydratase (A9MWI4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A9MWI4
- Type
- protein
- Length
- 440 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xF2f87f077Bf4C1656e09B41684f4F18Dd78B5BC2
- Molecule
- D-serine dehydratase
- UniProt
- A9MWI4
- 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 | A9MWI4 |
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 | 33 | empty |
| 2 | 194 | 0.47 | 0.75 | 27 | 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 A9MWI4
- Elsewhere: UniProt A9MWI4 · AlphaFold DB A9MWI4
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