Research workbench
AlphaFold monomer V2.0 prediction for protease htpx homolog (B5XJV3)
Analyse AlphaFold monomer V2.0 prediction for protease htpx homolog (B5XJV3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B5XJV3
- Type
- protein
- Length
- 298 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5e58272ea25a05e06901A2eAe9f63939b344e0c6
- Molecule
- Protease htpx homolog
- UniProt
- B5XJV3
- Pockets
- 4 · best druggability 0.69
Structure
1 distinct chain · 68% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protease htpx homolog | protein | 298 | 68% helix, 5% strand | B5XJV3 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 51 | 0.69 | 0.98 | 18 | empty |
| 2 | 380 | 0.64 | 0.78 | 38 | empty |
| 3 | 143 | 0.46 | 0.77 | 18 | empty |
| 4 | 98 | 0.36 | 0.74 | 20 | 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 B5XJV3
- Elsewhere: UniProt B5XJV3 · AlphaFold DB B5XJV3
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