Research workbench
AlphaFold monomer V2.0 prediction for undecaprenyl-diphosphatase (B5E1R8)
Analyse AlphaFold monomer V2.0 prediction for undecaprenyl-diphosphatase (B5E1R8) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B5E1R8
- Type
- protein
- Length
- 281 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xF8cD1d8d93E9783063700De244A6e3cf6A195579
- Molecule
- Undecaprenyl-diphosphatase
- UniProt
- B5E1R8
- Pockets
- 3 · best druggability 0.77
Structure
1 distinct chain · 78% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Undecaprenyl-diphosphatase | protein | 281 | 78% helix, 1% strand | B5E1R8 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 516 | 0.77 | 0.85 | 51 | empty |
| 2 | 53 | 0.34 | 0.79 | 15 | empty |
| 3 | 62 | 0.33 | 0.77 | 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 B5E1R8
- Elsewhere: UniProt B5E1R8 · AlphaFold DB B5E1R8
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