5jqi

X-ray diffraction
1.96Å resolution

Crystal structure of FimH A62S from E. coli UTI89 bound to FimG N-terminal extension

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Type 1 fimbriae minor subunit FimG Chains: A, C, E, G
Molecule details ›
Chains: A, C, E, G
Length: 15 amino acids
Theoretical weight: 1.51 KDa
Source organism: Escherichia coli UTI89
Expression system: Not provided
UniProt:
  • Canonical: Q1R2J5 (Residues: 24-38; Coverage: 10%)
Gene names: UTI89_C5016, fimG
Type 1 fimbiral adhesin FimH Chains: B, D, F, H
Molecule details ›
Chains: B, D, F, H
Length: 279 amino acids
Theoretical weight: 29.05 KDa
Source organism: Escherichia coli UTI89
Expression system: Escherichia coli
UniProt:
  • Canonical: Q1R2J4 (Residues: 22-300; Coverage: 99%)
Gene names: UTI89_C5017, fimH
Sequence domains:
Structure domains: Fimbrial-type adhesion domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P1
Unit cell:
a: 56.44Å b: 75.56Å c: 78.44Å
α: 68.35° β: 69° γ: 77.43°
R-values:
R R work R free
0.191 0.189 0.239
Expression systems:
  • Not provided
  • Escherichia coli