PDBe 2nul

X-ray diffraction
2.1Å resolution

PEPTIDYLPROLYL ISOMERASE FROM E. COLI

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (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