2x7k

X-ray diffraction
1.15Å resolution

The crystal structure of PPIL1 in complex with cyclosporine A suggests a binding mode for SKIP

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
Non-polymer only dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peptidyl-prolyl cis-trans isomerase-like 1 Chain: A
Molecule details ›
Chain: A
Length: 166 amino acids
Theoretical weight: 18.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y3C6 (Residues: 1-166; Coverage: 100%)
Gene names: CGI-124, CYPL1, PPIL1, UNQ2425/PRO4984
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: BESSY BEAMLINE 14.2
Spacegroup: P21212
Unit cell:
a: 103.218Å b: 35.701Å c: 45.851Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.129 0.128 0.149
Expression systems:
  • Escherichia coli
  • Not provided