› 1lys

X-ray diffraction
1.72Å resolution

X-RAY STRUCTURE OF A MONOCLINIC FORM OF HEN EGG-WHITE LYSOZYME CRYSTALLIZED AT 313K. COMPARISON OF TWO INDEPENDENT MOLECULES

Released:
DOI: 10.2210/pdb1lys/pdb
PDB entry 1lys coloured by chain, front view.
PDB entry 1lys coloured by chain, side view.
PDB entry 1lys coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
X-ray structure of a monoclinic form of hen egg-white lysozyme crystallized at 313 K. Comparison of two independent molecules.
Harata K
Acta Crystallogr D Biol Crystallogr 50 250-7 (1994)
PMID: 15299435

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: 27.23Å b: 63.66Å c: 59.12Å
α: 90° β: 92.9° γ: 90°
R-values:
R R work R free
0.187 0.187 not available
Expression system: Not provided

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Citations

2 review citations

Interactions of protein antigens with antibodies.
Davies et al. (1996)
1 more

17 mentions without citation

Progress in small-angle scattering from biological solutions at high-brilliance synchrotrons.
Tuukkanen et al. (2017)
16 more