PDBe 254l

X-ray diffraction
1.9Å resolution

LYSOZYME

Released:
Source organism: Escherichia virus T4
Primary publication:
A relationship between protein stability and protein function.
Proc. Natl. Acad. Sci. U.S.A. 92 452-6 (1995)
PMID: 7831309

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: 18.6 KDa
Source organism: Escherichia virus T4
Expression system: Escherichia coli
UniProt:
  • Canonical: P00720 (Residues: 1-164; Coverage: 100%)
Gene name: E
Sequence domains: Phage lysozyme
Structure domains: Lysozyme

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P3221
Unit cell:
a: 61Å b: 61Å c: 97.2Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.158 0.158 not available
Expression system: Escherichia coli