X-ray diffraction
2.56Å resolution

Structure of the 2TEL crystallization module fused to T4 lysozyme with an Ala-Gly-Pro linker.

Primary publication:
Polymer-driven crystallization.
Protein Sci. 16 2542-51 (2007)
PMID: 17962407

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:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Transcription factor ETV6 Chains: A, C
Molecule details ›
Chains: A, C
Length: 77 amino acids
Theoretical weight: 9.25 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
  • Canonical: P41212 (Residues: 47-123; Coverage: 17%)
Gene names: ETV6, TEL, TEL1
Structure domains: Transcription Factor, Ets-1
Endolysin Chains: B, D
Molecule details ›
Chains: B, D
Length: 241 amino acids
Theoretical weight: 27.72 KDa
Source organism: Escherichia virus T4
Expression system: Escherichia coli
  • Canonical: P00720 (Residues: 2-162; Coverage: 98%)
Gene name: E
Sequence domains: Phage lysozyme
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: P32
Unit cell:
a: 122.62Å b: 122.62Å c: 53.586Å
α: 90° β: 90° γ: 120°
R R work R free
0.213 0.211 0.252
Expression system: Escherichia coli