› 1uwf

X-ray diffraction
1.69Å resolution

1.7 A resolution structure of the receptor binding domain of the FimH adhesin from uropathogenic E. coli

Released:
DOI: 10.2210/pdb1uwf/pdb
PDB 1uwf coloured by chain and viewed from the front.
PDB 1uwf coloured by chain and viewed from the side.
PDB 1uwf coloured by chain and viewed from the top.
Source organism: Escherichia coli J96
Primary publication:
Receptor binding studies disclose a novel class of high-affinity inhibitors of the Escherichia coli FimH adhesin.
Bouckaert J, Berglund J, Schembri M, De Genst E, Cools L, Wuhrer M, Hung CS, Pinkner J, Slättegård R, Zavialov A, Choudhury D, Langermann S, Hultgren SJ, Wyns L, Klemm P, Oscarson S, Knight SD, De Greve H
Mol. Microbiol. 55 441-55 (2005)
PMID: 15659162

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Type 1 fimbrin D-mannose specific adhesin Chain: A
Molecule details ›
Chain: A
Length: 158 amino acids
Theoretical weight: 16.92 KDa
Source organism: Escherichia coli J96
Expression system: Escherichia coli
UniProt:
  • Canonical: P08191 (Residues: 22-179; Coverage: 57%)
Gene names: JW4283, b4320, fimH
Sequence domains: FimH, mannose binding
Structure domains: Fimbrial-type adhesion domain

Ligands and Environments

2 bound ligands:
Ligand DEG 1 x DEG
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P212121
Unit cell:
a: 39.906Å b: 41.636Å c: 97.07Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.179 0.218
Expression system: Escherichia coli

Quick links

Citations

64 review citations

Glycan-mediated molecular interactions in bacterial pathogenesis.
Lee et al. (2022)
63 more

19 mentions without citation

Neutralizing Antibodies Against Allosteric Proteins: Insights From a Bacterial Adhesin.
Sokurenko et al. (2022)
18 more