› 4x5q

X-ray diffraction
1.12Å resolution

Crystal structure of FimH in complex with 5-nitro-indolinylphenyl alpha-D-mannopyranoside

Released:
DOI: 10.2210/pdb4x5q/pdb
PDB 4x5q coloured by chain and viewed from the front.
PDB 4x5q coloured by chain and viewed from the side.
PDB 4x5q coloured by chain and viewed from the top.
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:
  • 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: 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 3XN 1 x 3XN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P212121
Unit cell:
a: 48.46Å b: 56.16Å c: 61.54Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.107 0.106 0.129
Expression system: Escherichia coli

Quick links

Citations

4 review citations

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