Structure analysis

Crystal Structure of the Grb2 SH2 Domain in Complex with a Flexible Ac-pY-E-N-NH2 Tripeptide Mimic

X-ray diffraction
2.02Å resolution
Source organism: Homo sapiens
Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 6100 Å2
Buried surface area: 1200 Å2
Dissociation area: 400 Å2
Dissociation energy (ΔGdiss): -2 kcal/mol
Dissociation entropy (TΔSdiss): 6 kcal/mol
Interface energy (ΔGint): -26 kcal/mol
Symmetry number: 1
Assembly 2
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Multimeric state: homo dimer
Accessible surface area: 10300 Å2
Buried surface area: 4400 Å2
Dissociation area: 1,100 Å2
Dissociation energy (ΔGdiss): 6 kcal/mol
Dissociation entropy (TΔSdiss): 11 kcal/mol
Interface energy (ΔGint): -55 kcal/mol
Symmetry number: 2

Macromolecules

Chain: A
Length: 117 amino acids
Theoretical weight: 13.76 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P62993 (Residues: 53-163; Coverage: 51%)
Gene names: ASH, GRB2
Pfam: SH2 domain
InterPro:
CATH: SHC Adaptor Protein

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