› 1el1

X-ray diffraction
1.9Å resolution

X-RAY CRYSTAL STRUCTURE ANALYSIS OF CANINE MILK LYSOZYME (HOLO-TYPE)

Released:
DOI: 10.2210/pdb1el1/pdb
PDB entry 1el1 coloured by chain, front view.
PDB entry 1el1 coloured by chain, side view.
PDB entry 1el1 coloured by chain, top view.
Source organism: Canis lupus familiaris
Primary publication:
Calcium Induced Conformational Changes of Canine Milk Lysozyme Revealed by Structural and Thermodynamical Evidences
Koshiba T, Yao M, Tanaka I, Nitta K
To be published

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:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160549 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysozyme C, milk isozyme Chains: A, B
Molecule details ›
Chains: A, B
Length: 130 amino acids
Theoretical weight: 14.58 KDa
Source organism: Canis lupus familiaris
Expression system: Escherichia coli
UniProt:
  • Canonical: P81708 (Residues: 1-129; Coverage: 100%)
Sequence domains: C-type lysozyme/alpha-lactalbumin family
Structure domains: Lysozyme

Ligands and Environments

1 bound ligand:
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-18B
Spacegroup: P32
Unit cell:
a: 31.3Å b: 31.3Å c: 202.5Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.159 0.159 0.257
Expression system: Escherichia coli

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