› 1uic

X-ray diffraction
1.95Å resolution

ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE AND CHARGED SIDE CHAINS

Released:
DOI: 10.2210/pdb1uic/pdb
PDB entry 1uic coloured by chain, front view.
PDB entry 1uic coloured by chain, side view.
PDB entry 1uic coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
Analysis of the stability of mutant lysozymes at position 15 using X-ray crystallography.
Ohmura T, Ueda T, Motoshima H, Tamura T, Imoto T
J Biochem 122 512-7 (1997)
PMID: 9348077

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: 14.26 KDa
Source organism: Gallus gallus
Expression system: Saccharomyces cerevisiae
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
Spacegroup: P43212
Unit cell:
a: 79.56Å b: 79.56Å c: 37.84Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.169 not available
Expression system: Saccharomyces cerevisiae

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Citations

6 citation in other articles

Analysis of the relationship between enzyme activity and its internal motion using nuclear magnetic resonance: 15N relaxation studies of wild-type and mutant lysozyme.
Mine et al. (1999)
5 more