› 4css

X-ray diffraction
1.07Å resolution

Crystal structure of FimH in complex with a sulfonamide biphenyl alpha D-mannoside

Released:
DOI: 10.2210/pdb4css/pdb
PDB 4css coloured by chain and viewed from the front.
PDB 4css coloured by chain and viewed from the side.
PDB 4css coloured by chain and viewed from the top.
Source organism: Escherichia coli K-12
Primary publication:
FimH Antagonists: Bioisosteres To Improve the in Vitro and in Vivo PK/PD Profile.
Kleeb S, Pang L, Mayer K, Eris D, Sigl A, Preston RC, Zihlmann P, Sharpe T, Jakob RP, Abgottspon D, Hutter AS, Scharenberg M, Jiang X, Navarra G, Rabbani S, Smiesko M, Lüdin N, Bezençon J, Schwardt O, Maier T, Ernst B
J. Med. Chem. (2015)
PMID: 25666045

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: 163 amino acids
Theoretical weight: 17.44 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 CWX 1 x CWX
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P212121
Unit cell:
a: 48.384Å b: 56.234Å c: 61.595Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.113 0.112 0.132
Expression system: Escherichia coli

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Citations

10 review citations

Toward Glycomaterials with Selectivity as Well as Affinity.
Richards et al. (2021)
9 more