PDBe 1ojn

X-ray diffraction
1.6Å resolution

SPECIFICITY AND MECHANISM OF STREPTOCOCCUS PNEUMONIAE HYALURONATE LYASE: COMPLEX OF THE TYR408PHE MUTANT WITH 6-SULPHATED CHONDROITIN DISACCHARIDE

Released:

Function and Biology Details

Reaction catalysed:
Cleaves hyaluronate chains at a beta-D-GlcNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine
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
Macromolecule:
Hyaluronate lyase Chain: A
Molecule details ›
Chain: A
Length: 731 amino acids
Theoretical weight: 83.55 KDa
Source organism: Streptococcus pneumoniae
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q54873 (Residues: 285-1009; Coverage: 70%)
Gene name: SP_0314
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 83.912Å b: 104.2Å c: 101.499Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.194 0.209
Expression system: Escherichia coli BL21