5la4

X-ray diffraction
1.9Å resolution

Crystal structure of apo human proheparanase

Released:

Function and Biology Details

Reaction catalysed:
Endohydrolysis of (1->4)-beta-D-glycosidic bonds of heparan sulfate chains in heparan sulfate proteoglycan
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-195098 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Heparanase Chain: A
Molecule details ›
Chain: A
Length: 509 amino acids
Theoretical weight: 57.73 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: Q9Y251 (Residues: 36-543; Coverage: 100%)
Gene names: HEP, HPA, HPA1, HPR1, HPSE, HPSE1, HSE1
Sequence domains: Glycosyl hydrolase family 79, N-terminal domain

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P212121
Unit cell:
a: 50.501Å b: 88.061Å c: 120.497Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.185 0.227
Expression system: Trichoplusia ni