Structure analysis

Crystal structure of the complex between the EGFR kinase domain and a Mig6 peptide

X-ray diffraction
2.9Å resolution
Source organism: Homo sapiens
Assemblies composition:
hetero dimer (preferred)
monomeric
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1
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Multimeric state: hetero dimer
Accessible surface area: 14549.29 Å2
Buried surface area: 1827.15 Å2
Dissociation area: 913.58 Å2
Dissociation energy (ΔGdiss): 8.96 kcal/mol
Dissociation entropy (TΔSdiss): 9.53 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-132685
Assembly 2 (preferred)
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Multimeric state: hetero dimer
Accessible surface area: 14083.65 Å2
Buried surface area: 1784.23 Å2
Dissociation area: 892.11 Å2
Dissociation energy (ΔGdiss): 9.07 kcal/mol
Dissociation entropy (TΔSdiss): 9.35 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-132685
Assembly 3
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Multimeric state: monomeric
Accessible surface area: 12789.24 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-132671
Assembly 4
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Multimeric state: monomeric
Accessible surface area: 13581.44 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-132671

Macromolecules

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Chains: E, F
Length: 40 amino acids
Theoretical weight: 4.25 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q9UJM3 (Residues: 325-364; Coverage: 9%)
Gene names: ERRFI1, MIG6
Pfam: EGFR receptor inhibitor Mig-6

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