Function and Biology Details
Reaction catalysed:
Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Lysozyme g (preferred)
PDBe Complex ID:
PDB-CPX-108009 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Lysozyme g
Molecule details ›
Chain: A
Length: 187 amino acids
Theoretical weight: 21.09 KDa
Source organism: Salmo salar
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Transglycosylase SLT domain
Structure domains: Lysozyme
Length: 187 amino acids
Theoretical weight: 21.09 KDa
Source organism: Salmo salar
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
A6PZ97 (Residues: 22-200; Coverage: 100%)
Sequence domains: Transglycosylase SLT domain
Structure domains: Lysozyme
Inhibitor of g-type lysozyme
Molecule details ›
Chain: B
Length: 111 amino acids
Theoretical weight: 12.54 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Bacterial pre-peptidase C-terminal domain
Structure domains: Jelly Rolls
Length: 111 amino acids
Theoretical weight: 12.54 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: P76002 (Residues: 23-133; Coverage: 100%)
Sequence domains: Bacterial pre-peptidase C-terminal domain
Structure domains: Jelly Rolls
