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:
Biological process:
Cellular component:
Sequence domains:
- Polysaccharide lyase family 8-like, C-terminal
- Chondroitin AC/alginate lyase
- Polysaccharide lyase family 8, C-terminal
- Glycoside hydrolase-type carbohydrate-binding
- Polysaccharide lyase family 8, central domain
- Galactose mutarotase-like domain superfamily
- Polysaccharide lyase 8, N-terminal alpha-helical
- Polysaccharide lyase 8
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Hyaluronate lyase (preferred)
PDBe Complex ID:
PDB-CPX-176228 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hyaluronate lyase
Molecule details ›
Chain: A
Length: 721 amino acids
Theoretical weight: 82.15 KDa
Source organism: Streptococcus pneumoniae
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 721 amino acids
Theoretical weight: 82.15 KDa
Source organism: Streptococcus pneumoniae
Expression system: Escherichia coli
UniProt:
- Canonical:
Q54873 (Residues: 287-1007; Coverage: 70%)
Sequence domains:
- Polysaccharide lyase family 8, N terminal alpha-helical domain
- Polysaccharide lyase family 8, super-sandwich domain
- Polysaccharide lyase family 8, C-terminal beta-sandwich domain
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
ALS BEAMLINE 5.0.1
Spacegroup:
P212121
Expression system: Escherichia coli
