› 1j2a

X-ray diffraction
1.8Å resolution

Structure of E. coli cyclophilin B K163T mutant

Released:
DOI: 10.2210/pdb1j2a/pdb
PDB entry 1j2a coloured by chain, front view.
PDB entry 1j2a coloured by chain, side view.
PDB entry 1j2a coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Escherichia coli cyclophilin B binds a highly distorted form of trans-prolyl peptide isomer.
Konno M, Sano Y, Okudaira K, Kawaguchi Y, Yamagishi-Ohmori Y, Fushinobu S, Matsuzawa H
Eur J Biochem 271 3794-803 (2004)
PMID: 15355356

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-142738 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase A Chain: A
Molecule details ›
Chain: A
Length: 166 amino acids
Theoretical weight: 18.07 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AFL3 (Residues: 25-190; Coverage: 100%)
Gene names: JW3326, b3363, ppiA, rot, rotA
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: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P3221
Unit cell:
a: 82.55Å b: 82.55Å c: 52.35Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.201 0.201 0.225
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Interactions between folding factors and bacterial outer membrane proteins.
Mogensen et al. (2005)
1 more

3 mentions without citation

X-ray vs. NMR structures as templates for computational protein design.
Schneider et al. (2009)
2 more