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 dimer (preferred)
Assembly name:
Ig-like domain-containing protein and Lysozyme C (preferred)
PDBe Complex ID:
PDB-CPX-132863 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ig-like domain-containing protein
Molecule details ›
Chains: N, O
Length: 121 amino acids
Theoretical weight: 13.44 KDa
Source organism: Ginglymostoma cirratum
Expression system: Escherichia coli
UniProt:
Structure domains: Immunoglobulins
Length: 121 amino acids
Theoretical weight: 13.44 KDa
Source organism: Ginglymostoma cirratum
Expression system: Escherichia coli
UniProt:
- Canonical:
Q8AXH5 (Residues: 1-89, 90-112; Coverage: 99%)
Structure domains: Immunoglobulins
Lysozyme C
Molecule details ›
Chains: L, M
Length: 129 amino acids
Theoretical weight: 14.33 KDa
Source organism: Gallus gallus
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
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
X-ray source:
SSRL BEAMLINE BL9-2
Spacegroup:
P212121
Expression system: Escherichia coli
