› 4jkm

X-ray diffraction
2.26Å resolution

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:
hetero hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142640 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Beta-glucuronidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 602 amino acids
Theoretical weight: 69.09 KDa
Source organism: Clostridium perfringens str. 13
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8XP19 (Residues: 1-599; Coverage: 100%)
Gene names: CPE0147, bglR
Sequence domains:
Structure domains:
Maltose/maltodextrin-binding periplasmic protein Chains: C, D
Molecule details ›
Chains: C, D
Length: 400 amino acids
Theoretical weight: 44.27 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AEX9 (Residues: 27-392; Coverage: 99%)
Gene names: JW3994, b4034, malE
Sequence domains: Bacterial extracellular solute-binding protein
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: C2221
Unit cell:
a: 71.511Å b: 292.612Å c: 239.907Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.207 0.234
Expression system: Escherichia coli

Quick links

Citations

60 review citations

Comprehensive review of targeted therapy for colorectal cancer.
Xie et al. (2020)
59 more

8 mentions without citation

Crystal structures of MBP fusion proteins.
Waugh DS. (2016)
7 more

PDB-REDO

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