Structure analysis

Structure of the p53 cancer mutant Y220C with bound small molecule PhiKan7099

X-ray diffraction
1.35Å resolution
Source organism: Homo sapiens
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1
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Multimeric state: monomeric
Accessible surface area: 9974.19 Å2
Buried surface area: 279.4 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-138105
Assembly 2 (preferred)
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Multimeric state: monomeric
Accessible surface area: 10237.81 Å2
Buried surface area: 489.43 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-138105

Macromolecules

Chains: A, B
Length: 219 amino acids
Theoretical weight: 24.53 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04637 (Residues: 94-312; Coverage: 56%)
Gene names: P53, TP53
Pfam: P53 DNA-binding domain
InterPro:
CATH: Immunoglobulin-like

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