1n5b

X-ray diffraction
2Å resolution

Crystal Structure Of The Yersinia enterocolitica Molecular Chaperone Syce

Released:
Source organism: Yersinia enterocolitica
Primary publication:
Structure of the Yersinia enterocolitica molecular-chaperone protein SycE.
Acta Crystallogr D Biol Crystallogr 59 389-92 (2003)
PMID: 12554962

Function and Biology Details

Biochemical function:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-152021 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
YopE regulator Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 132 amino acids
Theoretical weight: 14.84 KDa
Source organism: Yersinia enterocolitica
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P31490 (Residues: 1-130; Coverage: 100%)
Gene names: YEP0052, yerA
Sequence domains: Tir chaperone protein (CesT) family
Structure domains: Yope Regulator; Chain: A,

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P212121
Unit cell:
a: 52.55Å b: 92.67Å c: 101.05Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.248 0.248 0.29
Expression system: Escherichia coli BL21(DE3)