› 4auj

X-ray diffraction
1.53Å resolution

FimH lectin domain co-crystal with a alpha-D-mannoside O-linked to para hydroxypropargyl phenyl

Released:
DOI: 10.2210/pdb4auj/pdb
PDB 4auj coloured by chain and viewed from the front.
PDB 4auj coloured by chain and viewed from the side.
PDB 4auj 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:
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 UTI89
Expression system: Escherichia coli BL21(DE3)
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

1 bound ligand:
Ligand HNW 1 x HNW
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P212121
Unit cell:
a: 32.92Å b: 42.29Å c: 96.34Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.16 0.185
Expression system: Escherichia coli BL21(DE3)

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Citations

5 review citations

Mannose-derived FimH antagonists: a promising anti-virulence therapeutic strategy for urinary tract infections and Crohn's disease.
Mydock-McGrane et al. (2016)
4 more

1 mention without citation

Sites for Dynamic Protein-Carbohydrate Interactions of O- and C-Linked Mannosides on the E. coli FimH Adhesin.
Touaibia et al. (2017)