› 1hen

X-ray diffraction
1.8Å resolution

STRUCTURAL AND THERMODYNAMIC ANALYSIS OF COMPENSATING MUTATIONS WITHIN THE CORE OF CHICKEN EGG WHITE LYSOZYME

Released:
DOI: 10.2210/pdb1hen/pdb
PDB entry 1hen coloured by chain, front view.
PDB entry 1hen coloured by chain, side view.
PDB entry 1hen coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
Structural and thermodynamic analysis of compensating mutations within the core of chicken egg white lysozyme.
Wilson KP, Malcolm BA, Matthews BW
J Biol Chem 267 10842-9 (1992)
PMID: 1587860

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
Expression system: Not provided
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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELLIOTT GX-21
Spacegroup: P43212
Unit cell:
a: 79.1Å b: 79.1Å c: 37.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.152 not available not available
Expression system: Not provided

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Citations

4 review citations

Missense meanderings in sequence space: a biophysical view of protein evolution.
DePristo et al. (2005)
3 more