Neutron Diffraction
2.2Å resolution

Neutron crystallographic structure of perdeuterated T4 lysozyme cysteine-free pseudo-wild type at cryogenic temperature


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:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Endolysin Chain: A
Molecule details ›
Chain: A
Length: 164 amino acids
Theoretical weight: 18.63 KDa
Source organism: Escherichia virus T4
Expression system: Escherichia coli
  • Canonical: P00720 (Residues: 1-164; Coverage: 100%)
Gene name: E
Sequence domains: Phage lysozyme

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Spacegroup: P3221
Unit cell:
a: 61.5Å b: 61.5Å c: 95.9Å α: 90° β: 90° γ: 120°
R R work R free 0.243 0.242 0.28
Expression system: Escherichia coli