Research workbench
AlphaFold monomer V2.0 prediction for dtdp-4-dehydrorhamnose 3,5-epimerase (P9WH11)
Analyse AlphaFold monomer V2.0 prediction for dtdp-4-dehydrorhamnose 3,5-epimerase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P9WH11
- Type
- protein
- Length
- 202 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xE1b961cFdddF7335AbA492F1fc32079dEd2c4285
- Molecule
- Dtdp-4-dehydrorhamnose 3,5-epimerase
- UniProt
- P9WH11
- Pockets
- 1 · best druggability 0.45
Structure
1 distinct chain · 16% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dtdp-4-dehydrorhamnose 3,5-epimerase | protein | 202 | 16% helix, 37% strand | P9WH11 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 109 | 0.45 | 0.79 | 24 | 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 P9WH11
- Elsewhere: UniProt P9WH11 · AlphaFold DB P9WH11
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