5jhe

X-ray diffraction
1.8Å resolution

The Crystal Structure of the Saccharomyces cerevisiae Co-Chaperone Cpr7

Released:
Entry authors: Yu Q, Xu L

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase CYP7 Chain: A
Molecule details ›
Chain: A
Length: 397 amino acids
Theoretical weight: 45.74 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P47103 (Residues: 1-393; Coverage: 100%)
Gene names: CPR7, J1585, YJR032W
Sequence domains:
Structure domains: Cyclophilin-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: P42
Unit cell:
a: 75.332Å b: 75.332Å c: 100.794Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.185 0.211
Expression system: Escherichia coli BL21(DE3)