2iff

X-ray diffraction
2.65Å resolution

STRUCTURE OF AN ANTIBODY-LYSOZYME COMPLEX: EFFECT OF A CONSERVATIVE MUTATION

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-208265 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
IGG1 HYHEL-5 FAB (LIGHT CHAIN) Chain: L
Molecule details ›
Chain: L
Length: 212 amino acids
Theoretical weight: 23.33 KDa
Source organism: Mus musculus
Expression system: Not provided
Structure domains: Immunoglobulins
IGG1 HYHEL-5 FAB (HEAVY CHAIN) Chain: H
Molecule details ›
Chain: H
Length: 215 amino acids
Theoretical weight: 22.98 KDa
Source organism: Mus musculus
Expression system: Not provided
Structure domains: Immunoglobulins
Lysozyme C Chain: Y
Molecule details ›
Chain: Y
Length: 129 amino acids
Theoretical weight: 14.3 KDa
Source organism: Gallus gallus
Expression system: Saccharomyces cerevisiae
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
Spacegroup: P21
Unit cell:
a: 54.8Å b: 74.8Å c: 79Å
α: 90° β: 101.8° γ: 90°
Expression systems:
  • Not provided
  • Saccharomyces cerevisiae