Research workbench
AlphaFold monomer V2.0 prediction for rhamnulokinase (B1LMU4)
Analyse AlphaFold monomer V2.0 prediction for rhamnulokinase (B1LMU4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B1LMU4
- Type
- protein
- Length
- 489 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xC36Aec97B2480dC1460726322bd613ba289B263C
- Molecule
- Rhamnulokinase
- UniProt
- B1LMU4
- Pockets
- 6 · best druggability 0.75
Structure
1 distinct chain · 43% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Rhamnulokinase | protein | 489 | 43% helix, 21% strand | B1LMU4 |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 455 | 0.75 | 0.84 | 60 | empty |
| 2 | 82 | 0.46 | 0.81 | 19 | empty |
| 3 | 162 | 0.45 | 0.75 | 29 | empty |
| 4 | 51 | 0.31 | 0.77 | 14 | empty |
| 5 | 52 | 0.30 | 0.76 | 12 | 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 B1LMU4
- Elsewhere: UniProt B1LMU4 · AlphaFold DB B1LMU4
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