Research workbench
AlphaFold monomer V2.0 prediction for chaperone protein hsca (B7MIL6)
Analyse AlphaFold monomer V2.0 prediction for chaperone protein hsca (B7MIL6) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B7MIL6
- Type
- protein
- Length
- 616 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb3c0C983Fc44934AC589D7131C08a72544EBB92E
- Molecule
- Chaperone protein hsca
- UniProt
- B7MIL6
- Pockets
- 8 · best druggability 0.80
Structure
1 distinct chain · 40% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein hsca | protein | 616 | 40% helix, 27% strand | B7MIL6 |
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 501 | 0.80 | 0.87 | 67 | empty |
| 2 | 63 | 0.73 | 0.99 | 24 | empty |
| 3 | 105 | 0.49 | 0.80 | 19 | empty |
| 4 | 179 | 0.47 | 0.76 | 26 | empty |
| 5 | 71 | 0.45 | 0.82 | 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 B7MIL6
- Elsewhere: UniProt B7MIL6 · AlphaFold DB B7MIL6
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