1jtp

X-ray diffraction
1.9Å resolution

Degenerate interfaces in antigen-antibody complexes

Released:

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:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-226696 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Single-Domain Antibody Chains: A, B
Molecule details ›
Chains: A, B
Length: 148 amino acids
Theoretical weight: 15.76 KDa
Source organism: Camelus dromedarius
Expression system: Escherichia coli
Structure domains: Immunoglobulins
Lysozyme C Chains: L, M
Molecule details ›
Chains: L, M
Length: 129 amino acids
Theoretical weight: 14.23 KDa
Source organism: Meleagris gallopavo
UniProt:
  • Canonical: P00703 (Residues: 19-147; Coverage: 100%)
Gene name: LYZ
Sequence domains: C-type lysozyme/alpha-lactalbumin family
Structure domains: Lysozyme

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: P212121
Unit cell:
a: 67.123Å b: 69.375Å c: 113.231Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.184 0.229
Expression system: Escherichia coli