PDBe 1vdn

X-ray diffraction
1.6Å resolution

Crystal Structure Of Yeast Cyclophilin A Complexed With ACE-Ala-Ala-Pro-Ala-7-Amino-4-Methylcoumarin

Released:
Entry authors: Konno M, Shibano T, Okudaira K, Takahashi N

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peptidyl-prolyl cis-trans isomerase Chain: A
Molecule details ›
Chain: A
Length: 162 amino acids
Theoretical weight: 17.41 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P14832 (Residues: 1-162; Coverage: 100%)
Gene names: CPH1, CPR1, CYP1, SCC1, YD8358.10C, YDR155C
Sequence domains: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
Structure domains: Cyclophilin-like
(ACE)AAPA(MCM) Chain: B
Molecule details ›
Chain: B
Length: 6 amino acids
Theoretical weight: 512 Da
Source organism: Synthetic construct
Expression system: Not provided

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: P212121
Unit cell:
a: 31.737Å b: 40.009Å c: 112.736Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.199 0.237
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided