3mgw

X-ray diffraction
1.75Å resolution

Thermodynamics and structure of a salmon cold-active goose-type lysozyme

Released:
Source organism: Salmo salar
Primary publication:
Thermodynamics and structure of a salmon cold active goose-type lysozyme.
Comp Biochem Physiol B Biochem Mol Biol 156 254-63 (2010)
PMID: 20398783

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-108009 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysozyme g Chain: A
Molecule details ›
Chain: A
Length: 181 amino acids
Theoretical weight: 20.27 KDa
Source organism: Salmo salar
Expression system: Escherichia coli
UniProt:
  • Canonical: A6PZ97 (Residues: 22-200; Coverage: 100%)
Gene names: LOC100136420, LYG, lysG
Sequence domains: Transglycosylase SLT domain
Structure domains: Lysozyme

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: R3
Unit cell:
a: 103.15Å b: 103.15Å c: 48.67Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.178 0.176 0.215
Expression system: Escherichia coli