1xjt

X-ray diffraction
1.75Å resolution

Crystal structure of active 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
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174304 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
SAR-endolysin Chain: A
Molecule details ›
Chain: A
Length: 191 amino acids
Theoretical weight: 21.49 KDa
Source organism: Escherichia virus P1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q37875 (Residues: 1-185; Coverage: 100%)
Gene names: 17, lysa, lyz
Sequence domains: Phage lysozyme
Structure domains: Lysozyme

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID, APS BEAMLINE 14-BM-C
Spacegroup: P6522
Unit cell:
a: 66.871Å b: 66.871Å c: 166.796Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.209 0.208 0.238
Expression system: Escherichia coli