› 4r3e

X-ray diffraction
2Å resolution

Structure of the spliceosomal peptidyl-prolyl cis-trans isomerase Cwc27 from Homo sapiens

Released:
DOI: 10.2210/pdb4r3e/pdb
PDB entry 4r3e coloured by chain, front view.
PDB entry 4r3e coloured by chain, side view.
PDB entry 4r3e coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure and evolution of the spliceosomal peptidyl-prolyl cis-trans isomerase Cwc27.
Ulrich A, Wahl MC
Acta Crystallogr D Biol Crystallogr 70 3110-23 (2014)
PMID: 25478830

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

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180424 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Spliceosome-associated protein CWC27 homolog Chain: A
Molecule details ›
Chain: A
Length: 180 amino acids
Theoretical weight: 20.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6UX04 (Residues: 1-178; Coverage: 38%)
Gene names: CWC27, SDCCAG10, UNQ438/PRO871
Sequence domains: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
Structure domains: Cyclophilin-like

Ligands and Environments

1 bound ligand:
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: P65
Unit cell:
a: 85.86Å b: 85.86Å c: 55.02Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.174 0.172 0.217
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Microbial cyclophilins: specialized functions in virulence and beyond.
Dimou et al. (2017)
12 other articles

1 mention without citation

Structural and Functional Insights into Human Nuclear Cyclophilins.
Rajiv et al. (2018)