› 3lyt

X-ray diffraction
1.9Å resolution

COMPARISON OF RADIATION-INDUCED DECAY AND STRUCTURE REFINEMENT FROM X-RAY DATA COLLECTED FROM LYSOZYME CRYSTALS AT LOW AND AMBIENT TEMPERATURES

Released:
DOI: 10.2210/pdb3lyt/pdb
PDB entry 3lyt coloured by chain, front view.
PDB entry 3lyt coloured by chain, side view.
PDB entry 3lyt coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
Comparison of Radiation-Induced Decay and Structure Refinement from X-Ray Data Collected from Lysozyme Crystals at Low and Ambient Temperatures
Young ACM, Dewan JC, Nave C, Tilton RF
J Appl Crystallogr 26 309- (1993)

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 Chains: A, B
Molecule details ›
Chains: A, B
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
Spacegroup: P21
Unit cell:
a: 27.51Å b: 62.66Å c: 59.66Å
α: 90° β: 89.57° γ: 90°
R-values:
R R work R free
0.203 not available not available
Expression system: Not provided

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