Research workbench
AlphaFold monomer V2.0 prediction for chaperone protein hsca homolog (Q62IZ5)
Analyse AlphaFold monomer V2.0 prediction for chaperone protein hsca homolog (Q62IZ5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q62IZ5
- Type
- protein
- Length
- 622 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3c860Cd4B4aF5cd0B224EEce054f91b534Db0285
- Molecule
- Chaperone protein hsca homolog
- UniProt
- Q62IZ5
- Pockets
- 5 · best druggability 0.70
Structure
1 distinct chain · 41% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein hsca homolog | protein | 622 | 41% helix, 26% strand | Q62IZ5 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 54 | 0.70 | 0.98 | 22 | empty |
| 2 | 192 | 0.66 | 0.86 | 35 | empty |
| 3 | 146 | 0.66 | 0.87 | 26 | empty |
| 4 | 194 | 0.47 | 0.75 | 26 | empty |
| 5 | 90 | 0.41 | 0.78 | 19 | 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 Q62IZ5
- Elsewhere: UniProt Q62IZ5 · AlphaFold DB Q62IZ5
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