› 1lks

X-ray diffraction
1.1Å resolution

HEN EGG WHITE LYSOZYME NITRATE

Released:
DOI: 10.2210/pdb1lks/pdb
PDB entry 1lks coloured by chain, front view.
PDB entry 1lks coloured by chain, side view.
PDB entry 1lks coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
Structures of monoclinic lysozyme iodide at 1.6 A and of triclinic lysozyme nitrate at 1.1 A.
Steinrauf LK
Acta Crystallogr D Biol Crystallogr 54 767-80 (1998)
PMID: 9757091

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-132831 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysozyme C Chain: A
Molecule details ›
Chain: A
Length: 129 amino acids
Theoretical weight: 14.33 KDa
Source organism: Gallus gallus
UniProt:
  • Canonical: P00698 (Residues: 19-147; Coverage: 100%)
Gene name: LYZ
Sequence domains: C-type lysozyme/alpha-lactalbumin family
Structure domains: Lysozyme

Ligands and Environments

1 bound ligand:
Ligand NO3 6 x NO3
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P1
Unit cell:
a: 31.97Å b: 65.08Å c: 27.25Å
α: 94.57° β: 111.56° γ: 82.98°

Quick links

Citations

2 review citations

Why continuum electrostatics theories cannot explain biological structure, polyelectrolytes or ionic strength effects in ion-protein interactions.
Collins KD. (2012)
1 more

7 mentions without citation

Hypervalent nonbonded interactions of a divalent sulfur atom. Implications in protein architecture and the functions.
Iwaoka et al. (2012)
6 more