› 154l

X-ray diffraction
1.6Å resolution

THE REFINED STRUCTURES OF GOOSE LYSOZYME AND ITS COMPLEX WITH A BOUND TRISACCHARIDE SHOW THAT THE "GOOSE-TYPE LYSOZYMES LACK A CATALYTIC ASPARTATE

Released:
DOI: 10.2210/pdb154l/pdb
PDB entry 154l coloured by chain, front view.
PDB entry 154l coloured by chain, side view.
PDB entry 154l coloured by chain, top view.
Source organism: Anser anser anser
Primary publication:
The refined structures of goose lysozyme and its complex with a bound trisaccharide show that the "goose-type" lysozymes lack a catalytic aspartate residue.
Weaver LH, Grütter MG, Matthews BW
J Mol Biol 245 54-68 (1995)
PMID: 7823320

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:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132939 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Lysozyme g Chain: A
Molecule details ›
Chain: A
Length: 185 amino acids
Theoretical weight: 20.41 KDa
Source organism: Anser anser anser
Expression system: Not provided
UniProt:
  • Canonical: P00718 (Residues: 1-185; Coverage: 100%)
Sequence domains: Transglycosylase SLT domain
Structure domains: Lysozyme

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 38.3Å b: 65.4Å c: 44.7Å
α: 90° β: 117° γ: 90°
R-values:
R R work R free
0.159 not available not available
Expression system: Not provided

Quick links

Citations

9 review citations

Structures and mechanisms of glycosyl hydrolases.
Davies et al. (1995)
8 more

11 mentions without citation

Antimicrobial Proteins and Peptides in Avian Eggshell: Structural Diversity and Potential Roles in Biomineralization.
Moreau et al. (2022)
10 more