› 4yuh

X-ray diffraction
1.34Å resolution

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158766 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase A Chain: A
Molecule details ›
Chain: A
Length: 165 amino acids
Theoretical weight: 18.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P62937 (Residues: 1-165; Coverage: 100%)
Gene names: CYPA, PPIA
Sequence domains: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
Structure domains: Cyclophilin-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P212121
Unit cell:
a: 42.45Å b: 51.82Å c: 88.01Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.125 0.124 0.156
Expression system: Escherichia coli

Quick links

Citations

13 review citations

X-Ray Free-Electron Lasers for the Structure and Dynamics of Macromolecules.
Chapman HN. (2019)
12 more

1 mention without citation

Mapping the conformational landscape of a dynamic enzyme by multitemperature and XFEL crystallography.
Keedy et al. (2015)