Research workbench
AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase FKBP1B (Q8HYX6)
Analyse AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q8HYX6
- Type
- protein
- Length
- 108 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xC247c99E05131ed14368eDD5e659B4F41aFA32ab
- UniProt
- Q8HYX6
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 108 | — | Q8HYX6 |
Compared structures
- 8RRX · Structure of RyR1 reconstituted into lipid nanodisc in primed state in complex with Ca2+… · an experimental structure of the same protein · chain A against H, TM-score 0.96
- 8RS0 · Structure of RyR1 in detergent in primed state in complex with nanobody and FKBP · an experimental structure of the same protein · chain A against D, TM-score 0.96
- 8RRU · Structure of RyR1 reconstituted into lipid liposomes in primed state in complex with FKBP… · an experimental structure of the same protein · chain A against H, TM-score 0.95
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 Q8HYX6
- Elsewhere: UniProt Q8HYX6 · AlphaFold DB Q8HYX6
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