Research workbench
AlphaFold monomer V2.0 prediction for cytoplasmic trehalase (B5R404)
Analyse AlphaFold monomer V2.0 prediction for cytoplasmic trehalase (B5R404) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B5R404
- Type
- protein
- Length
- 549 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x26b4f882EF3Ad62CE99d00E3cC6F1F054c691CE6
- Molecule
- Cytoplasmic trehalase
- UniProt
- B5R404
- Pockets
- 6 · best druggability 0.76
Structure
1 distinct chain · 48% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytoplasmic trehalase | protein | 549 | 48% helix, 10% strand | B5R404 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 75 | 0.76 | 0.99 | 24 | empty |
| 2 | 258 | 0.65 | 0.83 | 40 | empty |
| 3 | 341 | 0.63 | 0.79 | 38 | empty |
| 4 | 92 | 0.39 | 0.77 | 16 | empty |
| 5 | 80 | 0.37 | 0.77 | 13 | 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 B5R404
- Elsewhere: UniProt B5R404 · AlphaFold DB B5R404
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