› 1lsp

X-ray diffraction
2.45Å resolution

THE CRYSTAL STRUCTURE OF A BULGECIN-INHIBITED G-TYPE LYSOZYME FROM THE EGG-WHITE OF THE AUSTRALIAN BLACK SWAN. A COMPARISON OF THE BINDING OF BULGECIN TO THREE MURAMIDASES

Released:
DOI: 10.2210/pdb1lsp/pdb
PDB entry 1lsp coloured by chain, front view.
PDB entry 1lsp coloured by chain, side view.
PDB entry 1lsp coloured by chain, top view.
Source organism: Cygnus atratus
Primary publication:
Structure of a bulgecin-inhibited g-type lysozyme from the egg white of the Australian black swan. A comparison of the binding of bulgecin to three muramidases.
Karlsen S, Hough E, Rao ZH, Isaacs NW
Acta Crystallogr D Biol Crystallogr 52 105-14 (1996)
PMID: 15299731

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-132938 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysozyme g Chain: A
Molecule details ›
Chain: A
Length: 185 amino acids
Theoretical weight: 20.43 KDa
Source organism: Cygnus atratus
UniProt:
  • Canonical: P00717 (Residues: 1-185; Coverage: 100%)
Sequence domains: Transglycosylase SLT domain
Structure domains: Lysozyme

Ligands and Environments

1 bound ligand:
Ligand BUL 1 x BUL
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21212
Unit cell:
a: 91.69Å b: 65.33Å c: 38.15Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 not available not available

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Citations

1 citations in other articles

Crystal structures of g-type lysozyme from Atlantic cod shed new light on substrate binding and the catalytic mechanism.
Helland et al. (2009)

2 mentions without citation

Crystal structures of the catalytic domain of a novel glycohydrolase family 23 chitinase from Ralstonia sp. A-471 reveals a unique arrangement of the catalytic residues for inverting chitin hydrolysis.
Arimori et al. (2013)
1 more