Structure analysis

Structure of the human Mdmx protein bound to the p53 tumor suppressor transactivation domain

X-ray diffraction
1.8Å resolution
Source organisms:
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: 5529.56 Å2
Buried surface area: 1024.02 Å2
Dissociation area: 512.01 Å2
Dissociation energy (ΔGdiss): 5.15 kcal/mol
Dissociation entropy (TΔSdiss): 7.28 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-138120
Assembly 2
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Multimeric state: hetero dimer
Accessible surface area: 5734.49 Å2
Buried surface area: 1118.86 Å2
Dissociation area: 559.43 Å2
Dissociation energy (ΔGdiss): 5.19 kcal/mol
Dissociation entropy (TΔSdiss): 7.68 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-138120

Macromolecules

Chains: A, M
Length: 130 amino acids
Theoretical weight: 14.77 KDa
Source organism: Danio rerio
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7ZUW7 (Residues: 15-129; Coverage: 23%)
Gene names: mdm4, mdmx
Pfam: SWIB/MDM2 domain
InterPro:
CATH: SWIB/MDM2 domain

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Chains: B, P
Length: 21 amino acids
Theoretical weight: 2.4 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P04637 (Residues: 17-37; Coverage: 5%)
Gene names: P53, TP53
Pfam: P53 transactivation motif
InterPro: p53 transactivation domain

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