Research workbench
AlphaFold monomer V2.0 prediction for urease accessory protein ureg (B1MB87)
Analyse AlphaFold monomer V2.0 prediction for urease accessory protein ureg (B1MB87) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B1MB87
- Type
- protein
- Length
- 230 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x028515Ca84017068CF074628B04aDe18e16adfD8
- Molecule
- Urease accessory protein ureg
- UniProt
- B1MB87
- Pockets
- 2 · best druggability 0.55
Structure
1 distinct chain · 40% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Urease accessory protein ureg | protein | 230 | 40% helix, 18% strand | B1MB87 |
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 | 187 | 0.55 | 0.80 | 18 | empty |
| 2 | 54 | 0.27 | 0.73 | 11 | 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 B1MB87
- Elsewhere: UniProt B1MB87 · AlphaFold DB B1MB87
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