› 2nul

X-ray diffraction
2.1Å resolution

PEPTIDYLPROLYL ISOMERASE FROM E. COLI

Released:
DOI: 10.2210/pdb2nul/pdb
PDB entry 2nul coloured by chain, front view.
PDB entry 2nul coloured by chain, side view.
PDB entry 2nul coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of cytoplasmic Escherichia coli peptidyl-prolyl isomerase: evidence for decreased mobility of loops upon complexation.
Edwards KJ, Ollis DL, Dixon NE
J Mol Biol 271 258-65 (1997)
PMID: 9268657

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150086 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase B Chain: A
Molecule details ›
Chain: A
Length: 164 amino acids
Theoretical weight: 18.17 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P23869 (Residues: 1-164; Coverage: 100%)
Gene names: JW0514, b0525, ppiB
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: RIGAKU RUH2R
Spacegroup: C2221
Unit cell:
a: 44.7Å b: 68.2Å c: 102Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.16 not available

Quick links

Citations

2 review citations

SAIL--stereo-array isotope labeling.
Kainosho et al. (2009)
1 more

7 mentions without citation

Microbial peptidyl-prolyl cis/trans isomerases (PPIases): virulence factors and potential alternative drug targets.
Ünal et al. (2014)
6 more