Research workbench
AlphaFold monomer V2.0 prediction for phosphoglucosamine mutase (B9KE78)
Analyse AlphaFold monomer V2.0 prediction for phosphoglucosamine mutase (B9KE78) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B9KE78
- Type
- protein
- Length
- 445 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x084C9507B8890B44F4aE79C08a93A4457A564360
- Molecule
- Phosphoglucosamine mutase
- UniProt
- B9KE78
- Pockets
- 4 · best druggability 0.61
Structure
1 distinct chain · 39% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphoglucosamine mutase | protein | 445 | 39% helix, 20% strand | B9KE78 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 466 | 0.61 | 0.76 | 50 | empty |
| 2 | 129 | 0.41 | 0.75 | 18 | empty |
| 3 | 95 | 0.36 | 0.74 | 20 | empty |
| 4 | 88 | 0.34 | 0.74 | 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 B9KE78
- Elsewhere: UniProt B9KE78 · AlphaFold DB B9KE78
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