X-ray diffraction
2.6Å resolution

Crystal Structure of Recombinant Human Cyclophilin J

Source organism: Homo sapiens
Primary publication:
Structure of recombinant human cyclophilin J, a novel member of the cyclophilin family.
Acta Crystallogr. D Biol. Crystallogr. 61 316-21 (2005)
PMID: 15735342

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Peptidyl-prolyl cis-trans isomerase-like 3 Chain: A
Molecule details ›
Chain: A
Length: 161 amino acids
Theoretical weight: 18.18 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
  • Canonical: Q9H2H8 (Residues: 1-161; Coverage: 100%)
Gene name: PPIL3
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: OTHER
Spacegroup: P3121
Unit cell:
a: 41.309Å b: 41.309Å c: 172.116Å
α: 90° β: 90° γ: 120°
R R work R free
0.181 0.175 0.236
Expression system: Escherichia coli BL21