1jef

X-ray diffraction
1.77Å resolution

TURKEY LYSOZYME COMPLEX WITH (GLCNAC)3

Released:
Source organism: Meleagris gallopavo
Primary publication:
X-ray structure of turkey-egg lysozyme complex with tri-N-acetylchitotriose. Lack of binding ability at subsite A.
Acta Crystallogr. D Biol. Crystallogr. 53 650-7 (1997)
PMID: 15299852

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
UniProt:
  • Canonical: P00703 (Residues: 19-147; Coverage: 100%)
Gene name: LYZ
Sequence domains: C-type lysozyme/alpha-lactalbumin family
Structure domains: Lysozyme

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELLIOTT GX-21
Spacegroup: C2
Unit cell:
a: 87.49Å b: 32.94Å c: 49Å
α: 90° β: 119.1° γ: 90°
R-values:
R R work R free
0.182 0.182 0.225