2fuq

X-ray diffraction
2.15Å resolution

Crystal Structure of Heparinase II

Released:

Function and Biology Details

Reactions catalysed:
Eliminative cleavage of polysaccharides containing (1->4)-linked D-glucuronate or L-iduronate residues and (1->4)-alpha-linked 2-sulfoamino-2-deoxy-6-sulfo-D-glucose residues to give oligosaccharides with terminal 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends
Elimination of sulfate, appears to act on linkages between N-acetyl-D-glucosamine and uronate. Product is an unsaturated sugar.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-111657 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Heparin and heparin-sulfate lyase Chains: A, B
Molecule details ›
Chains: A, B
Length: 747 amino acids
Theoretical weight: 84.71 KDa
Source organism: Pedobacter heparinus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: C6XZB6 (Residues: 26-772; Coverage: 100%)
Gene names: Phep_2408, hepB
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: MAN, GCU, XYS, RAM
3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P212121
Unit cell:
a: 70.046Å b: 119.339Å c: 200.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.195 0.235
Expression system: Escherichia coli BL21(DE3)