Research workbench
AlphaFold monomer V2.0 prediction for co-chaperone protein hscb homolog (Q2SXE1)
Analyse AlphaFold monomer V2.0 prediction for co-chaperone protein hscb homolog (Q2SXE1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q2SXE1
- Type
- protein
- Length
- 175 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbb2F1C7CB3A1eeFAc24fCa72cc627162D5413FD7
- Molecule
- Co-chaperone protein hscb homolog
- UniProt
- Q2SXE1
- Pockets
- 1 · best druggability 0.27
Structure
1 distinct chain · 75% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Co-chaperone protein hscb homolog | protein | 175 | 75% helix, 0% strand | Q2SXE1 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 54 | 0.27 | 0.73 | 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 Q2SXE1
- Elsewhere: UniProt Q2SXE1 · AlphaFold DB Q2SXE1
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