› 7m5i

X-ray diffraction
1.71Å resolution

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-101283 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endolysin Chains: A, B
Molecule details ›
Chains: A, B
Length: 160 amino acids
Theoretical weight: 17.94 KDa
Source organism: Escherichia coli O157 typing phage 15
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0F6R9G3 (Residues: 1-154; Coverage: 100%)
Gene names: ECTP15_02508, rrrD
Sequence domains: Phage lysozyme

Ligands and Environments

1 bound ligand:
Ligand PO4 4 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P3221
Unit cell:
a: 67.874Å b: 67.874Å c: 134.437Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.175 0.173 0.203
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Biocontrol Approaches against Escherichia coli O157:H7 in Foods.
Puligundla et al. (2022)
2 more

1 mention without citation

The Molecular Basis for Escherichia coli O157:H7 Phage FAHEc1 Endolysin Function and Protein Engineering to Increase Thermal Stability.
Love et al. (2021)