› 1l4i

X-ray diffraction
2.2Å resolution

Crystal Structure of the Periplasmic Chaperone SfaE

Released:
DOI: 10.2210/pdb1l4i/pdb
PDB entry 1l4i coloured by chain, front view.
PDB entry 1l4i coloured by chain, side view.
PDB entry 1l4i coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure of the S pilus periplasmic chaperone SfaE at 2.2 A resolution.
Knight SD, Choudhury D, Hultgren S, Pinkner J, Stojanoff V, Thompson A
Acta Crystallogr D Biol Crystallogr 58 1016-22 (2002)
PMID: 12037304

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158654 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Chaperone protein FocC Chains: A, B
Molecule details ›
Chains: A, B
Length: 206 amino acids
Theoretical weight: 22.75 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P62609 (Residues: 22-227; Coverage: 100%)
Gene name: focC
Sequence domains:
Structure domains: Immunoglobulins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X31
Spacegroup: P212121
Unit cell:
a: 53.5Å b: 84.24Å c: 97.34Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.19 0.244
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Immunoglobulin domains in Escherichia coli and other enterobacteria: from pathogenesis to applications in antibody technologies.
Bodelón et al. (2013)
4 more

5 mentions without citation

Functional and structural characterization of Vibrio cholerae extracellular serine protease B, VesB.
Gadwal et al. (2014)
4 more