1xju

X-ray diffraction
1.07Å resolution

Crystal structure of secreted inactive form of P1 phage endolysin Lyz

Released:

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:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-174304 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
SAR-endolysin Chains: A, B
Molecule details ›
Chains: A, B
Length: 163 amino acids
Theoretical weight: 18.48 KDa
Source organism: Escherichia virus P1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q37875 (Residues: 29-185; Coverage: 85%)
Gene names: 17, lysa, lyz
Sequence domains: Phage lysozyme
Structure domains: Lysozyme

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P21
Unit cell:
a: 33.349Å b: 59.786Å c: 76.228Å
α: 90° β: 102.51° γ: 90°
R-values:
R R work R free
0.134 0.133 0.153
Expression system: Escherichia coli