› 1zmf

X-ray diffraction
1.88Å resolution

C domain of human cyclophilin-33(hcyp33)

Released:
DOI: 10.2210/pdb1zmf/pdb
PDB entry 1zmf coloured by chain, front view.
PDB entry 1zmf coloured by chain, side view.
PDB entry 1zmf coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
1.88 A crystal structure of the C domain of hCyP33: a novel domain of peptidyl-prolyl cis-trans isomerase.
Wang T, Yun CH, Gu SY, Chang WR, Liang DC
Biochem Biophys Res Commun 333 845-9 (2005)
PMID: 15963461

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
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: 165 amino acids
Theoretical weight: 18.23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UNP9 (Residues: 137-301; Coverage: 55%)
Gene names: CYP33, PPIE
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: HOME SOURCE
Spacegroup: P42212
Unit cell:
a: 66.61Å b: 66.61Å c: 76.78Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.169 0.225
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Pro isomerization in MLL1 PHD3-bromo cassette connects H3K4me readout to CyP33 and HDAC-mediated repression.
Wang et al. (2010)
3 more

2 mentions without citation

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