2huk

X-ray diffraction
2Å resolution

Crystal structure of T4 Lysozyme V131C synthetic dimer

Released:
Source organism: Escherichia virus T4
Primary publication:
An approach to crystallizing proteins by synthetic symmetrization.
Proc Natl Acad Sci U S A 103 16230-5 (2006)
PMID: 17050682

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133029 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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 BL21(DE3)
UniProt:
  • Canonical: P00720 (Residues: 1-164; Coverage: 100%)
Gene name: E
Sequence domains: Phage lysozyme
Structure domains: Lysozyme

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: C2
Unit cell:
a: 184.267Å b: 29.408Å c: 31.243Å
α: 90° β: 97.39° γ: 90°
R-values:
R R work R free
0.181 0.178 0.24
Expression system: Escherichia coli BL21(DE3)