Research workbench
AlphaFold monomer V2.0 prediction for beta-phosphoglucomutase (O06995)
Analyse AlphaFold monomer V2.0 prediction for beta-phosphoglucomutase (O06995) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O06995
- Type
- protein
- Length
- 226 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBc0D917FA4795675935BEf33e3A0671BBDb3ebf1
- Molecule
- Beta-phosphoglucomutase
- UniProt
- O06995
- Pockets
- 2 · best druggability 0.70
Structure
1 distinct chain · 52% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-phosphoglucomutase | protein | 226 | 52% helix, 12% strand | O06995 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 122 | 0.70 | 0.92 | 36 | empty |
| 2 | 69 | 0.28 | 0.73 | 16 | empty |
Compared structures
- 3NAS · The crystal structure of beta-phosphoglucomutase from bacillus subtilis · an experimental structure of the same protein · chain A against B, TM-score 0.78
- 3NAS · The crystal structure of beta-phosphoglucomutase from Bacillus subtilis · an experimental structure of the same protein · chain A against B, TM-score 0.78
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 O06995
- Elsewhere: UniProt O06995 · AlphaFold DB O06995
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