› 4x50

X-ray diffraction
2Å resolution

Crystal structure of FimH in complex with biphenyl alpha-D-mannopyranoside

Released:
DOI: 10.2210/pdb4x50/pdb
PDB entry 4x50 coloured by chain, front view.
PDB entry 4x50 coloured by chain, side view.
PDB entry 4x50 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
Molecule details ›
Chains: A, B
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

1 bound ligand:
Ligand 3X8 2 x 3X8
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P212121
Unit cell:
a: 63.32Å b: 69.29Å c: 95.92Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.174 0.202
Expression system: Escherichia coli

Quick links

Citations

4 review citations

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

2 mentions without citation

Mutation of Tyr137 of the universal Escherichia coli fimbrial adhesin FimH relaxes the tyrosine gate prior to mannose binding.
Rabbani et al. (2017)
1 more