› 4x5r

X-ray diffraction
1.65Å resolution

Crystal structure of FimH in complex with a squaryl-phenyl alpha-D-mannopyranoside derivative

Released:
DOI: 10.2210/pdb4x5r/pdb
PDB entry 4x5r coloured by chain, front view.
PDB entry 4x5r coloured by chain, side view.
PDB entry 4x5r coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
The tyrosine gate of the bacterial lectin FimH: a conformational analysis by NMR spectroscopy and X-ray crystallography.
Fiege B, Rabbani S, Preston RC, Jakob RP, Zihlmann P, Schwardt O, Jiang X, Maier T, Ernst B
Chembiochem 16 1235-46 (2015)
PMID: 25940742

Function and Biology Details

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

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, C
Molecule details ›
Chains: A, B, C
Length: 160 amino acids
Theoretical weight: 17.09 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P08191 (Residues: 22-180; 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 3XO 3 x 3XO
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P212121
Unit cell:
a: 53.29Å b: 96.93Å c: 97.86Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.164 0.204
Expression system: Escherichia coli

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Citations

4 review citations

Pathoblockers or antivirulence drugs as a new option for the treatment of bacterial infections.
Calvert et al. (2018)
3 more