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:
hetero dimer (preferred)
Assembly name:
Fibronectin and Lysozyme C (preferred)
PDBe Complex ID:
PDB-CPX-132849 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Lysozyme C
Molecule details ›
Chains: A, B
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
Ugl-Y3
Molecule details ›
Chains: C, D
Length: 102 amino acids
Theoretical weight: 11.3 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Fibronectin type III domain
Structure domains: Immunoglobulins
Length: 102 amino acids
Theoretical weight: 11.3 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P02751 (Residues: 1538-1561, 1562-1592, 1593-1631; Coverage: 4%)
Sequence domains: Fibronectin type III domain
Structure domains: Immunoglobulins
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
wwPDB Validation report is not available for this entry.
X-ray source:
AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup:
P212121
Expression system: Escherichia coli
