Research workbench
AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase a (P62938)
Analyse AlphaFold monomer V2.0 prediction for peptidyl-prolyl cis-trans isomerase a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P62938
- Type
- protein
- Length
- 165 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x54FBC17A5C73fF6f44d925D726c013269Fd7F733
- Molecule
- Peptidyl-prolyl cis-trans isomerase a
- UniProt
- P62938
Structure
1 distinct chain · 14% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidyl-prolyl cis-trans isomerase a | protein | 165 | 14% helix, 33% strand | P62938 |
Compared structures
- 5HSV · X-ray structure of a cypa-alisporivir complex at 1.5 ångström resolution · an experimental structure of the same protein · chain A against A, TM-score 0.99
- 5HSV · X-Ray structure of a CypA-Alisporivir complex at 1.5 angstrom resolution · an experimental structure of the same protein · chain A against A, TM-score 0.99
- 9BGH · Crystal structure of KRAS G12D in a transition state mimetic complex with CYPA and… · an experimental structure of the same protein · chain A against B, TM-score 0.98
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 P62938
- Elsewhere: UniProt P62938 · AlphaFold DB P62938
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