1sf6

X-ray powder diffraction

BINDING OF N,N',N"-TRIACETYLCHITOTRIOSE TO HEW LYSOZYME: A POWDER DIFFRACTION STUDY

Released:
Source organism: Gallus gallus
Primary publication:
Binding of N-acetylglucosamine oligosaccharides to hen egg-white lysozyme: a powder diffraction study.
Acta Crystallogr D Biol Crystallogr 61 22-32 (2005)
PMID: 15608372

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)
Assembly name:
PDBe Complex ID:
PDB-CPX-132831 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Lysozyme C Chain: A
Molecule details ›
Chain: A
Length: 129 amino acids
Theoretical weight: 14.33 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

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

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X3B1
Spacegroup: P43212
Unit cell:
a: 78.77Å b: 78.77Å c: 38.368Å
α: 90° β: 90° γ: 90°
Expression system: Escherichia coli