PDBe 1dpx

X-ray diffraction
1.65Å resolution

STRUCTURE OF HEN EGG-WHITE LYSOZYME

Released:
Source organism: Gallus gallus
Primary publication:
Crystallization, structure solution and refinement of hen egg-white lysozyme at pH 8.0 in the presence of MPD.
Acta Crystallogr. D Biol. Crystallogr. 56 952-8 (2000)
PMID: 10944331

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. 
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysozyme C Chain: A
Molecule details ›
Chain: A
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

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: P43212
Unit cell:
a: 77.05Å b: 77.05Å c: 37.21Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.187 0.246