PDBe 1zkf

X-ray diffraction
2.55Å resolution

Cyrstal Structure of Human Cyclophilin-A in Complex with suc-AGPF-pNA

Released:
Entry authors: Eisenmesser EZ, Thai V, Pozharski E, Kern D

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Suc-ALA-GLY-PRO-PHE-pNA Chains: C, D
Molecule details ›
Chains: C, D
Length: 6 amino acids
Theoretical weight: 611 Da
Source organism: Synthetic construct
Expression system: Not provided
Peptidyl-prolyl cis-trans isomerase A Chains: A, B
Molecule details ›
Chains: A, B
Length: 165 amino acids
Theoretical weight: 18.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
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: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 35.757Å b: 108.82Å c: 118.726Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.168 0.21
Expression systems:
  • Not provided
  • Escherichia coli BL21(DE3)