› 3lpf

X-ray diffraction
2.26Å resolution

Structure of E. coli beta-Glucuronidase bound with a novel, potent inhibitor 1-((6,7-dimethyl-2-oxo-1,2-dihydroquinolin-3-yl)methyl)-1-(2-hydroxyethyl)-3-(3-methoxyphenyl)thiourea

Released:
DOI: 10.2210/pdb3lpf/pdb
PDB entry 3lpf coloured by chain, front view.
PDB entry 3lpf coloured by chain, side view.
PDB entry 3lpf coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Alleviating cancer drug toxicity by inhibiting a bacterial enzyme.
Wallace BD, Wang H, Lane KT, Scott JE, Orans J, Koo JS, Venkatesh M, Jobin C, Yeh LA, Mani S, Redinbo MR
Science 330 831-5 (2010)
PMID: 21051639

Function and Biology Details

Reaction catalysed: 
A beta-D-glucuronoside + H(2)O = D-glucuronate + an alcohol
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138786 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-glucuronidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 605 amino acids
Theoretical weight: 69.36 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P05804 (Residues: 1-603; Coverage: 100%)
Gene names: JW1609, b1617, gurA, gusA, uidA
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand Z77 2 x Z77
1 modified residue:
Ligand MSE 26 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: C2
Unit cell:
a: 168.058Å b: 77.409Å c: 126.152Å
α: 90° β: 124.66° γ: 90°
R-values:
R R work R free
0.211 0.209 0.249
Expression system: Escherichia coli

Quick links

Citations

238 review citations

The gut microbiota, bacterial metabolites and colorectal cancer.
Louis et al. (2014)
237 more

19 mentions without citation

The Role of Gut Microbial β-Glucuronidase in Estrogen Reactivation and Breast Cancer.
Sui et al. (2021)
18 more