X-ray diffraction
1.69Å resolution

Crystal structure of the modular Cpl-1 endolysin complexed with a peptidoglycan analogue (E94Q mutant in complex with a tetrasaccharide- pentapeptide)


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
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Lysozyme Chain: A
Molecule details ›
Chain: A
Length: 339 amino acids
Theoretical weight: 39.22 KDa
Source organism: Streptococcus phage Cp-1
Expression system: Escherichia coli DH1
  • Canonical: P15057 (Residues: 1-339; Coverage: 100%)
Gene names: 22, CPL1
Sequence domains:
Structure domains:

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: C2221
Unit cell:
a: 79.52Å b: 97.39Å c: 127.14Å
α: 90° β: 90° γ: 90°
R R work R free
0.187 0.187 0.22
Expression system: Escherichia coli DH1