› 4buq

X-ray diffraction
2.2Å resolution

Crystal structure of wild type FimH lectin domain in complex with heptyl alpha-D-mannopyrannoside

Released:
DOI: 10.2210/pdb4buq/pdb
PDB 4buq coloured by chain and viewed from the front.
PDB 4buq coloured by chain and viewed from the side.
PDB 4buq coloured by chain and viewed from the top.
Source organism: Escherichia coli UTI89
Primary publication:
Validation of Reactivity Descriptors to Assess the Aromatic Stacking within the Tyrosine Gate of FimH.
Roos G, Wellens A, Touaibia M, Yamakawa N, Geerlings P, Roy R, Wyns L, Bouckaert J
ACS Med Chem Lett 4 1085-90 (2013)
PMID: 24900609

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
FimH mannose-binding domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 158 amino acids
Theoretical weight: 16.92 KDa
Source organism: Escherichia coli UTI89
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A2IC68 (Residues: 10-167; Coverage: 70%)
Gene name: fimH
Sequence domains: FimH, mannose binding
Structure domains: Fimbrial-type adhesion domain

Ligands and Environments

1 bound ligand:
Ligand KGM 2 x KGM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: P212121
Unit cell:
a: 60.305Å b: 68.07Å c: 95.607Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.202 0.256
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

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

11 mentions without citation

Targeting Dynamical Binding Processes in the Design of Non-Antibiotic Anti-Adhesives by Molecular Simulation-The Example of FimH.
Krammer et al. (2018)
10 more