› 3k2c

X-ray diffraction
1.95Å resolution

Crystal structure of peptidyl-prolyl cis-trans isomerase from Encephalitozoon cuniculi at 1.9 A resolution

Released:
DOI: 10.2210/pdb3k2c/pdb
PDB entry 3k2c coloured by chain, front view.
PDB entry 3k2c coloured by chain, side view.
PDB entry 3k2c coloured by chain, top view.
Source organism: Encephalitozoon cuniculi
Entry authors: SSGCID, Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186087 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 193 amino acids
Theoretical weight: 21.36 KDa
Source organism: Encephalitozoon cuniculi
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8SRE1 (Residues: 1-172; Coverage: 100%)
Gene names: CPR1, ECU08_0470
Sequence domains: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
Structure domains: Cyclophilin-like

Ligands and Environments

3 bound ligands:
Ligand PG5 2 x PG5
Ligand EDO 2 x EDO
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P1
Unit cell:
a: 38.81Å b: 73.86Å c: 63.59Å
α: 90.01° β: 79.1° γ: 90.02°
R-values:
R R work R free
0.166 0.163 0.216
Expression system: Escherichia coli

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