› 3uch

X-ray diffraction
2.5Å resolution

Crystal structure of a peptidyl-prolyl cis-trans isomerase E (PPIE) from Homo sapiens at 2.50 A resolution

Released:
DOI: 10.2210/pdb3uch/pdb
PDB entry 3uch coloured by chain, front view.
PDB entry 3uch coloured by chain, side view.
PDB entry 3uch coloured by chain, top view.
Source organism: Homo sapiens
Entry authors: Joint Center for Structural Genomics (JCSG), Partnership for T-Cell Biology (TCELL)

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo trimer
Assembly name:
PDBe Complex ID:
PDB-CPX-194001 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase E Chain: A
Molecule details ›
Chain: A
Length: 174 amino acids
Theoretical weight: 19.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UNP9 (Residues: 129-301; Coverage: 58%)
Gene names: CYP33, PPIE
Sequence domains: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
Structure domains: Cyclophilin-like

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 5 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: I213
Unit cell:
a: 116.232Å b: 116.232Å c: 116.232Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.19 0.214
Expression system: Escherichia coli

Quick links