› 1lzn

Neutron Diffraction
1.7Å resolution

NEUTRON STRUCTURE OF HEN EGG-WHITE LYSOZYME

Released:
DOI: 10.2210/pdb1lzn/pdb
PDB entry 1lzn coloured by chain, front view.
PDB entry 1lzn coloured by chain, side view.
PDB entry 1lzn coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
Quasi-Laue neutron-diffraction study of the water arrangement in crystals of triclinic hen egg-white lysozyme.
Bon C, Lehmann MS, Wilkinson C
Acta Crystallogr D Biol Crystallogr 55 978-87 (1999)
PMID: 10216294

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

3 bound ligands:
Ligand NO3 5 x NO3
Ligand NA 1 x NA
Ligand DOD 115 x DOD
No modified residues

Experiments and Validation Details

Spacegroup: P1
Unit cell:
a: 27.28Å b: 32.04Å c: 34.27Å α: 88.8° β: 108.8° γ: 111.6°
R-values:
R R work R free 0.204 0.204 0.221

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Citations

7 review citations

Carbon-oxygen hydrogen bonding in biological structure and function.
Horowitz et al. (2012)
6 more

10 mentions without citation

Evaluation of models determined by neutron diffraction and proposed improvements to their validation and deposition.
Liebschner et al. (2018)
9 more