1lzy

X-ray diffraction
1.55Å resolution

X-RAY STRUCTURE OF TURKEY EGG LYSOZYME COMPLEX WITH DI-N-ACETYLCHITOBIOSE. RECOGNITION AND BINDING OF ALPHA-ANOMERIC FORM

Released:
Source organism: Meleagris gallopavo
Primary publication:
X-ray structure of monoclinic turkey egg lysozyme at 1.3 A resolution.
Acta Crystallogr. D Biol. Crystallogr. 49 497-504 (1993)
PMID: 15299509

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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Lysozyme C Chain: A
Molecule details ›
Chain: A
Length: 129 amino acids
Theoretical weight: 14.23 KDa
Source organism: Meleagris gallopavo
Expression system: Not provided
UniProt:
  • Canonical: P00703 (Residues: 19-147; Coverage: null%)
Gene name: LYZ
Structure domains: Lysozyme

Ligands and Environments

Carbohydrate polymer : NEW Components: NDG, NAG
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 38.22Å b: 33.14Å c: 46Å
α: 90° β: 109.9° γ: 90°
R-values:
R R work R free
0.175 0.175 not available
Expression system: Not provided