X-ray diffraction
1.4Å resolution

Crystal structure of CBM32-4 from the Clostridium perfringens NagH

Entry authors: Grondin JM, Ficko-Blean E, Boraston AB, Smith SP

Function and Biology Details

Reaction catalysed:
Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Hyaluronoglucosaminidase Chain: A
Molecule details ›
Chain: A
Length: 173 amino acids
Theoretical weight: 19 KDa
Source organism: Clostridium perfringens ATCC 13124
Expression system: Escherichia coli
  • Canonical: A0A0H2YRL1 (Residues: 1063-1229; Coverage: 11%)
Gene names: CPF_0184, nagH
Structure domains: Galactose-binding domain-like

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: OTHER
Spacegroup: P21
Unit cell:
a: 35.102Å b: 64.709Å c: 37.723Å
α: 90° β: 94.52° γ: 90°
R R work R free
0.15 0.149 0.171
Expression system: Escherichia coli