1ljn

X-ray diffraction
1.19Å resolution

Crystal Structure of Turkey Egg Lysozyme Complex with Di-N-acetylchitobiose at 1.19A Resolution

Released:
Source organism: Meleagris gallopavo
Primary publication:
Crystallographic dissection of the thermal motion of protein-sugar complex.
Proteins 48 53-62 (2002)
PMID: 12012337

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:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132924 (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: ENRAF-NONIUS FR571
Spacegroup: P21
Unit cell:
a: 38.2Å b: 33.29Å c: 46.21Å
α: 90° β: 109.94° γ: 90°
R-values:
R R work R free
0.104 0.103 0.138