Research workbench
AlphaFold monomer V2.0 prediction for co-chaperone protein hscb homolog (Q65RT1)
Analyse AlphaFold monomer V2.0 prediction for co-chaperone protein hscb homolog (Q65RT1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q65RT1
- Type
- protein
- Length
- 173 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6DAA77C4263E74E745cA9c4D8E291e57e8991Cf5
- Molecule
- Co-chaperone protein hscb homolog
- UniProt
- Q65RT1
Structure
1 distinct chain · 79% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Co-chaperone protein hscb homolog | protein | 173 | 79% helix, 0% strand | Q65RT1 |
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 Q65RT1
- Elsewhere: UniProt Q65RT1 · AlphaFold DB Q65RT1
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.