› 1tr7

X-ray diffraction
2.1Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140004 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Type 1 fimbrin D-mannose specific adhesin Chains: A, B
Molecule details ›
Chains: A, B
Length: 164 amino acids
Theoretical weight: 17.75 KDa
Source organism: Escherichia coli
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

3 bound ligands:
Ligand DEG 2 x DEG
Ligand CAC 1 x CAC
Ligand MPD 1 x MPD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: C2
Unit cell:
a: 134.1Å b: 29.2Å c: 93.3Å
α: 90° β: 92.2° γ: 90°
R-values:
R R work R free
0.17 0.17 0.2
Expression system: Escherichia coli

Quick links

Citations

71 review citations

The biology and future prospects of antivirulence therapies.
Cegelski et al. (2008)
70 more

8 mentions without citation

Intervening with urinary tract infections using anti-adhesives based on the crystal structure of the FimH-oligomannose-3 complex.
Wellens et al. (2008)
7 more