1hmu

X-ray diffraction
2Å resolution

ACTIVE SITE OF CHONDROITINASE AC LYASE REVEALED BY THE STRUCTURE OF ENZYME-OLIGOSACCHARIDE COMPLEXES AND MUTAGENESIS

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (4 distinct):
Chondroitinase-AC Chain: A
Molecule details ›
Chain: A
Length: 700 amino acids
Theoretical weight: 79.8 KDa
Source organism: Pedobacter heparinus
Expression system: Pedobacter heparinus
UniProt:
  • Canonical: Q59288 (Residues: 1-700; Coverage: 100%)
Gene names: Phep_0786, chnAC, cslA
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: MAN, GCU, XYP, MXY, RAM
Carbohydrate polymer : NEW Components: MAN, GCU, RAM
Carbohydrate polymer : NEW Components: ASG, GCD
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: P43212
Unit cell:
a: 86.9Å b: 86.9Å c: 192.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.227 0.227 0.266
Expression system: Pedobacter heparinus