Structure analysis

Structures of Grb2-SH2 Domain and AICD peptide Complexes Reveal a Conformational Switch and Their Functional Implications.

X-ray diffraction
2.3Å 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: 6621.5 Å2
Buried surface area: 903.2 Å2
Dissociation area: 451.6 Å2
Dissociation energy (ΔGdiss): 6.48 kcal/mol
Dissociation entropy (TΔSdiss): 6.83 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-138364

Macromolecules

Chain: A
Length: 101 amino acids
Theoretical weight: 11.73 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P62993 (Residues: 55-152; Coverage: 45%)
Gene names: ASH, GRB2
Pfam: SH2 domain
InterPro:
CATH: SH2 domain

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C31
Chain: L
Length: 9 amino acids
Theoretical weight: 1.14 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P05067 (Residues: 754-762; Coverage: 1%)
Gene names: A4, AD1, APP

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