2pe4

X-ray diffraction
2Å resolution

Structure of Human Hyaluronidase 1, a Hyaluronan Hydrolyzing Enzyme Involved in Tumor Growth and Angiogenesis

Released:

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:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171396 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Hyaluronidase-1 Chain: A
Molecule details ›
Chain: A
Length: 424 amino acids
Theoretical weight: 47.41 KDa
Source organism: Homo sapiens
Expression system: Drosophila melanogaster
UniProt:
  • Canonical: Q12794 (Residues: 22-435; Coverage: 100%)
Gene names: HYAL1, LUCA1
Sequence domains: Hyaluronidase
Structure domains: Aldolase class I

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer : NEW Components: NAG
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P3221
Unit cell:
a: 92.05Å b: 92.05Å c: 143.81Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.19 0.19 0.23
Expression system: Drosophila melanogaster