Structure analysis

Crystal Structure of the Grb2 SH2 Domain in Complex with a Cyclopropyl-constrained Ac-pTyr-Ile-Asn-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

Binding statistics and energies are not available for this assembly
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 6100 Å2
Buried surface area: 850 Å2
Dissociation area: 400 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 6 kcal/mol
Interface energy (ΔGint): 1 kcal/mol
Symmetry number: 1
Assembly 3
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Multimeric state: homo dimer

Binding statistics and energies are not available for this assembly

Macromolecules

Chains: A, B
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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