Structure analysis

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

X-ray diffraction
2.56Å resolution
Source organism: Homo sapiens
Assembly composition:
hetero dimer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero dimer
Accessible surface area: 17114.48 Å2
Buried surface area: 1610.0 Å2
Dissociation area: 673.16 Å2
Dissociation energy (ΔGdiss): -4.4 kcal/mol
Dissociation entropy (TΔSdiss): 11.04 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-133024
Assembly 2
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Multimeric state: hetero dimer
Accessible surface area: 16925.8 Å2
Buried surface area: 1737.56 Å2
Dissociation area: 670.99 Å2
Dissociation energy (ΔGdiss): -4.46 kcal/mol
Dissociation entropy (TΔSdiss): 11.05 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-133024

Macromolecules

Chains: A, C
Length: 77 amino acids
Theoretical weight: 9.25 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P41212 (Residues: 47-123; Coverage: 17%)
Gene names: ETV6, TEL, TEL1
Pfam: Sterile alpha motif (SAM)/Pointed domain
InterPro:
CATH: Transcription Factor, Ets-1
SCOP: Pointed domain

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Chains: B, D
Length: 241 amino acids
Theoretical weight: 27.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00720 (Residues: 2-162; Coverage: 98%)
Gene name: E
Pfam: Phage lysozyme
InterPro:
CATH:

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