Structure analysis

The 1.9A crystal structure of humanized Xenopus Mdm2 with nutlin-3a

X-ray diffraction
1.91Å resolution
Source organism: Xenopus laevis
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 5500 Å2
Buried surface area: 950 Å2
Dissociation area: 400 Å2
Dissociation energy (ΔGdiss): 2 kcal/mol
Dissociation entropy (TΔSdiss): 5 kcal/mol
Interface energy (ΔGint): -20 kcal/mol
Symmetry number: 1

Macromolecules

Chain: A
Length: 86 amino acids
Theoretical weight: 9.96 KDa
Source organism: Xenopus laevis
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P56273 (Residues: 20-105; Coverage: 18%)
Gene name: mdm2
Pfam: SWIB/MDM2 domain
InterPro:
CATH: MDM2

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