1ja2

X-ray powder diffraction

BINDING OF N-ACETYLGLUCOSAMINE TO CHICKEN EGG LYSOZYME: A POWDER DIFFRACTION STUDY

Released:
Source organism: Gallus gallus
Primary publication:
Binding of N-acetylglucosamine to chicken egg lysozyme: a powder diffraction study.
Acta Crystallogr. D Biol. Crystallogr. 57 1836-42 (2001)
PMID: 11717496

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:
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
Expression system: Escherichia coli
UniProt:
  • Canonical: P00698 (Residues: 19-147; Coverage: 100%)
Gene name: LYZ
Sequence domains: C-type lysozyme/alpha-lactalbumin family

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X3B1
Spacegroup: P43212
Unit cell:
a: 78.569Å b: 78.569Å c: 38.513Å
α: 90° β: 90° γ: 90°
Expression system: Escherichia coli