› 1xyh

X-ray diffraction
2.6Å resolution

Crystal Structure of Recombinant Human Cyclophilin J

Released:
DOI: 10.2210/pdb1xyh/pdb
PDB entry 1xyh coloured by chain, front view.
PDB entry 1xyh coloured by chain, side view.
PDB entry 1xyh coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of recombinant human cyclophilin J, a novel member of the cyclophilin family.
Huang LL, Zhao XM, Huang CQ, Yu L, Xia ZX
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:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190548 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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
UniProt:
  • 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-values:
R R work R free
0.181 0.175 0.236
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

The emerging role of peptidyl-prolyl isomerase chaperones in tau oligomerization, amyloid processing, and Alzheimer's disease.
Blair et al. (2015)
1 more

1 mention without citation

Roles of Prolyl Isomerases in RNA-Mediated Gene Expression.
Thapar R. (2015)