Research workbench
AlphaFold monomer V2.0 prediction for L-rhamnonate dehydratase (B5R264)
Analyse AlphaFold monomer V2.0 prediction for L-rhamnonate dehydratase (B5R264) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B5R264
- Type
- protein
- Length
- 405 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4d3Bd79Ba2ACACeE4ea169Badb24A7837154dEcf
- Molecule
- L-rhamnonate dehydratase
- UniProt
- B5R264
- Pockets
- 2 · best druggability 0.70
Structure
1 distinct chain · 37% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-rhamnonate dehydratase | protein | 405 | 37% helix, 18% strand | B5R264 |
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 | 50 | 0.70 | 0.98 | 16 | empty |
| 2 | 195 | 0.50 | 0.76 | 22 | 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 B5R264
- Elsewhere: UniProt B5R264 · AlphaFold DB B5R264
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