Research workbench
AlphaFold monomer V2.0 prediction for L-rhamnose isomerase (B1LMU3)
Analyse AlphaFold monomer V2.0 prediction for L-rhamnose isomerase (B1LMU3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B1LMU3
- Type
- protein
- Length
- 419 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x661f92Fc5950020C7aB410B5F5b9a3f429F49Ae5
- Molecule
- L-rhamnose isomerase
- UniProt
- B1LMU3
- Pockets
- 5 · best druggability 0.53
Structure
1 distinct chain · 46% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-rhamnose isomerase | protein | 419 | 46% helix, 12% strand | B1LMU3 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 169 | 0.53 | 0.79 | 27 | empty |
| 2 | 81 | 0.43 | 0.80 | 25 | empty |
| 3 | 88 | 0.40 | 0.77 | 22 | empty |
| 4 | 88 | 0.35 | 0.74 | 15 | empty |
| 5 | 73 | 0.30 | 0.73 | 19 | 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 B1LMU3
- Elsewhere: UniProt B1LMU3 · AlphaFold DB B1LMU3
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