PDBe 135l

X-ray diffraction
1.3Å resolution

X-RAY STRUCTURE OF MONOCLINIC TURKEY EGG LYSOZYME AT 1.3 ANGSTROMS RESOLUTION

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. 
Biological process:
Cellular component:

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: 14.23 KDa
Source organism: Meleagris gallopavo
Expression system: Not provided
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

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 38.07Å b: 33.2Å c: 46.12Å
α: 90° β: 110.06° γ: 90°
R-values:
R R work R free
0.189 0.189 not available
Expression system: Not provided