1cwc

X-ray diffraction
1.86Å resolution

IMPROVED BINDING AFFINITY FOR CYCLOPHILIN A BY A CYCLOSPORIN DERIVATIVE SINGLY MODIFIED AT ITS EFFECTOR DOMAIN

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-158777 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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
CYCLOSPORIN A Chain: C
Molecule details ›
Chain: C
Length: 11 amino acids
Theoretical weight: 1.23 KDa
Source organism: Tolypocladium inflatum
Expression system: Not provided

Ligands and Environments

No bound ligands

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 36.394Å b: 61.132Å c: 73.362Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.177 not available
Expression systems:
  • Escherichia coli
  • Not provided