2wfj

X-ray diffraction
0.75Å resolution

Atomic resolution crystal structure of the PPIase domain of human cyclophilin G in complex with cyclosporin A.

Released:

Function and Biology Details

Reaction catalysed:
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peptidyl-prolyl cis-trans isomerase G Chain: A
Molecule details ›
Chain: A
Length: 179 amino acids
Theoretical weight: 19.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13427 (Residues: 1-177; Coverage: 24%)
Gene name: PPIG
Sequence domains: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
Structure domains: Cyclophilin-like
CYCLOSPORIN A Chain: B
Molecule details ›
Chain: B
Length: 11 amino acids
Theoretical weight: 1.22 KDa
Source organism: Tolypocladium inflatum
Expression system: Not provided

Ligands and Environments

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P212121
Unit cell:
a: 37.319Å b: 64.913Å c: 69.285Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.112 not available 0.129
Expression systems:
  • Escherichia coli
  • Not provided