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X-ray powder diffraction

Synchrotron X-ray Powder Diffraction Study of Hexagonal Turkey Egg-white Lysozyme

Released:
DOI: 10.2210/pdb1xft/pdb
PDB entry 1xft coloured by chain, front view.
PDB entry 1xft coloured by chain, side view.
PDB entry 1xft coloured by chain, top view.
Source organism: Meleagris gallopavo
Primary publication:
Synchrotron X-ray powder diffraction study of hexagonal turkey egg-white lysozyme.
Margiolaki I, Wright JP, Fitch AN, Fox GC, Von Dreele RB
Acta Crystallogr D Biol Crystallogr 61 423-32 (2005)
PMID: 15805597

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-132924 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysozyme C Chain: A
Molecule details ›
Chain: A
Length: 129 amino acids
Theoretical weight: 14.23 KDa
Source organism: Meleagris gallopavo
UniProt:
  • Canonical: P00703 (Residues: 19-147; Coverage: 100%)
Gene name: LYZ
Sequence domains: C-type lysozyme/alpha-lactalbumin family

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID31
Spacegroup: P6122
Unit cell:
a: 71.086Å b: 71.086Å c: 85.028Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.113 not available not available

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Citations

1 review citation

In Quest for Improved Drugs against Diabetes: The Added Value of X-ray Powder Diffraction Methods.
Karavassili et al. (2017)
5 other articles

1 mention without citation

Synchrotron X-ray powder diffraction study of hexagonal turkey egg-white lysozyme.
Margiolaki et al. (2005)