› 1v9t

X-ray diffraction
1.7Å resolution

Structure of E. coli cyclophilin B K163T mutant bound to succinyl-ALA-PRO-ALA-P-nitroanilide

Released:
DOI: 10.2210/pdb1v9t/pdb
PDB entry 1v9t coloured by chain, front view.
PDB entry 1v9t coloured by chain, side view.
PDB entry 1v9t 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

Assemblies composition:
monomeric
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142739 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peptidyl-prolyl cis-trans isomerase A Chains: A, B
Molecule details ›
Chains: A, B
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
(SIN)APA(NIT) Chain: C
Molecule details ›
Chain: C
Length: 5 amino acids
Theoretical weight: 477 Da
Source organism: Escherichia coli
Expression system: Not provided

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: P32
Unit cell:
a: 79.28Å b: 79.28Å c: 56.63Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.184 0.184 0.221
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

2 review citations

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

2 mentions without citation

Discovery of Nicotinamide Adenine Dinucleotide Binding Proteins in the Escherichia coli Proteome Using a Combined Energetic- and Structural-Bioinformatics-Based Approach.
Zeng et al. (2017)
1 more