Structure analysis

THE CRYSTAL STRUCTURE OF AN EPH RECEPTOR SAM DOMAIN REVEALS A MECHANISM FOR MODULAR DIMERIZATION.

X-ray diffraction
2Å resolution
Source organism: Mus musculus
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 7721.84 Å2
Buried surface area: 2041.57 Å2
Dissociation area: 1,020.78 Å2
Dissociation energy (ΔGdiss): 7.23 kcal/mol
Dissociation entropy (TΔSdiss): 10.41 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-169847

Macromolecules

Chain: A
Length: 94 amino acids
Theoretical weight: 10.27 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q03137 (Residues: 888-981; Coverage: 10%)
Gene names: Epha4, Sek, Sek1
Pfam: SAM domain (Sterile alpha motif)
InterPro:
CATH: Transcription Factor, Ets-1
SCOP: SAM (sterile alpha motif) domain

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