PDBe 2hum

X-ray diffraction
2.35Å resolution

Crystal structure of T4 Lysozyme D72C 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
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endolysin Chains: A, B
Molecule details ›
Chains: A, B
Length: 164 amino acids
Theoretical weight: 18.62 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: ALS BEAMLINE 8.2.2
Spacegroup: P21
Unit cell:
a: 55.306Å b: 55.907Å c: 80.292Å
α: 90° β: 108.13° γ: 90°
R-values:
R R work R free
0.243 0.239 0.304
Expression system: Escherichia coli BL21(DE3)