1c08

X-ray diffraction
2.3Å resolution

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 trimer (preferred)
PDBe Complex ID:
PDB-CPX-132836 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Ig kappa chain V-V region L7 Chain: A
Molecule details ›
Chain: A
Length: 107 amino acids
Theoretical weight: 11.62 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P01642 (Residues: 21-115; Coverage: 100%)
Gene name: Gm10881
Sequence domains: Immunoglobulin V-set domain
Structure domains: Immunoglobulins
Ig heavy chain V region 36-60 Chain: B
Molecule details ›
Chain: B
Length: 114 amino acids
Theoretical weight: 12.8 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P01823 (Residues: 1-113; Coverage: 100%)
Sequence domains: Immunoglobulin V-set domain
Structure domains: Immunoglobulins
Lysozyme C Chain: C
Molecule details ›
Chain: C
Length: 129 amino acids
Theoretical weight: 14.33 KDa
Source organism: Gallus gallus
UniProt:
  • Canonical: P00698 (Residues: 19-147; Coverage: 100%)
Gene name: LYZ
Sequence domains: C-type lysozyme/alpha-lactalbumin family
Structure domains: Lysozyme

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MACSCIENCE
Spacegroup: P41212
Unit cell:
a: 57.208Å b: 57.208Å c: 236.071Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.235 0.175
Expression system: Escherichia coli