› 2o4w

X-ray diffraction
1.9Å 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-133020 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endolysin Chain: A
Molecule details ›
Chain: A
Length: 171 amino acids
Theoretical weight: 19.15 KDa
Source organism: Tequatrovirus T4
Expression system: Escherichia coli
UniProt:
  • Canonical: P00720 (Residues: 13-164, 1-11; Coverage: 99%)
Gene name: E
Structure domains: Lysozyme

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P3221
Unit cell:
a: 60.118Å b: 60.118Å c: 96.531Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.176 0.175 0.213
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Circular permutation: a different way to engineer enzyme structure and function.
Yu et al. (2011)
20 other articles

3 mentions without citation

Exploring subdomain cooperativity in T4 lysozyme I: structural and energetic studies of a circular permutant and protein fragment.
Cellitti et al. (2007)
2 more