Research workbench
AlphaFold monomer V2.0 prediction for dtdp-4-dehydrorhamnose 3-epimerase (Q9L9E5)
Analyse AlphaFold monomer V2.0 prediction for dtdp-4-dehydrorhamnose 3-epimerase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9L9E5
- Type
- protein
- Length
- 207 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x661f92Fc5950020C7aB410B5F5b9a3f429F49Ae5
- Molecule
- Dtdp-4-dehydrorhamnose 3-epimerase
- UniProt
- Q9L9E5
- Pockets
- 2 · best druggability 0.46
Structure
1 distinct chain · 13% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dtdp-4-dehydrorhamnose 3-epimerase | protein | 207 | 13% helix, 39% strand | Q9L9E5 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 100 | 0.46 | 0.80 | 26 | empty |
| 2 | 63 | 0.34 | 0.77 | 19 | empty |
Compared structures
- 2C0Z · The 1.6 A resolution crystal structure of NovW: a 4-keto-6-deoxy sugar epimerase from the… · an experimental structure of the same protein · chain A against A, TM-score 0.91
- 2C0Z · The 1.6 a resolution crystal structure of novw: a 4-keto-6- deoxy sugar epimerase from… · an experimental structure of the same protein · chain A against A, TM-score 0.91
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 Q9L9E5
- Elsewhere: UniProt Q9L9E5 · AlphaFold DB Q9L9E5
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