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:
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-208240 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Immunoglobulin kappa constant
Molecule details ›
Chain: A
Length: 214 amino acids
Theoretical weight: 23.58 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
Sequence domains: Immunoglobulin C1-set domain
Structure domains: Immunoglobulins
Length: 214 amino acids
Theoretical weight: 23.58 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
- Canonical:
P01837 (Residues: 1-107; Coverage: 100%)
Sequence domains: Immunoglobulin C1-set domain
Structure domains: Immunoglobulins
Lysozyme C
Molecule details ›
Chain: C
Length: 129 amino acids
Theoretical weight: 14.33 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli
UniProt:
Sequence domains: C-type lysozyme/alpha-lactalbumin family
Structure domains: Lysozyme
Length: 129 amino acids
Theoretical weight: 14.33 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli
UniProt:
- Canonical: P00698 (Residues: 19-147; Coverage: 100%)
Sequence domains: C-type lysozyme/alpha-lactalbumin family
Structure domains: Lysozyme
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Spacegroup:
P42212
Expression system: Escherichia coli
