PDBe 2lzm

X-ray diffraction
1.7Å resolution

STRUCTURE OF BACTERIOPHAGE T4 LYSOZYME REFINED AT 1.7 ANGSTROMS RESOLUTION

Released:
Source organism: Enterobacteria phage T4
Primary publication:
Structure of bacteriophage T4 lysozyme refined at 1.7 A resolution.
J. Mol. Biol. 193 189-99 (1987)
PMID: 3586019

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:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endolysin Chain: A
Molecule details ›
Chain: A
Length: 164 amino acids
Theoretical weight: 18.66 KDa
Source organism: Enterobacteria phage T4
Expression system: Not provided
UniProt:
  • Canonical: P00720 (Residues: 1-164; Coverage: 100%)
Gene name: E
Sequence domains: Phage lysozyme
Structure domains: Lysozyme

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3221
Unit cell:
a: 61.2Å b: 61.2Å c: 96.8Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.193 not available not available
Expression system: Not provided