Research workbench
AlphaFold monomer V2.0 prediction for dtdp-4-dehydrorhamnose 3,5-epimerase (P37763)
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
- P37763
- Type
- protein
- Length
- 328 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5Be6db7bf0250FDCB4deFDb7f993cB6C300c26C2
- Molecule
- Dtdp-4-dehydrorhamnose 3,5-epimerase
- UniProt
- P37763
- Pockets
- 2 · best druggability 0.70
Structure
1 distinct chain · 9% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dtdp-4-dehydrorhamnose 3,5-epimerase | protein | 328 | 9% helix, 26% strand | P37763 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 699 | 0.70 | 0.77 | 49 | empty |
| 2 | 118 | 0.56 | 0.84 | 26 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 P37763
- Elsewhere: UniProt P37763 · AlphaFold DB P37763
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