› 1uia

X-ray diffraction
1.76Å resolution

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

Released:
DOI: 10.2210/pdb1uia/pdb
PDB entry 1uia coloured by chain, front view.
PDB entry 1uia coloured by chain, side view.
PDB entry 1uia coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
Fluctuations in free or substrate-complexed lysozyme and a mutant of it detected on x-ray crystallography and comparison with those detected on NMR.
Ohmura T, Motoshima H, Ueda T, Imoto T
J Biochem 131 701-4 (2002)
PMID: 11983077

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: 127 amino acids
Theoretical weight: 14.04 KDa
Source organism: Gallus gallus
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: P00698 (Residues: 19-147; Coverage: 98%)
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: 79.72Å b: 79.72Å c: 37.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.18 not available
Expression system: Saccharomyces cerevisiae

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Citations

1 citations in other articles

Systematic comparison of crystal and NMR protein structures deposited in the protein data bank.
Sikic et al. (2010)