PDBe 150l

X-ray diffraction
2.2Å resolution

CONSERVATION OF SOLVENT-BINDING SITES IN 10 CRYSTAL FORMS OF T4 LYSOZYME

Released:
Source organism: Escherichia virus T4
Primary publication:
Conservation of solvent-binding sites in 10 crystal forms of T4 lysozyme.
Protein Sci. 3 1031-9 (1994)
PMID: 7920248

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 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 164 amino acids
Theoretical weight: 18.64 KDa
Source organism: Escherichia virus 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: P212121
Unit cell:
a: 72.2Å b: 73.8Å c: 150.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 not available not available
Expression system: Not provided