Structure analysis

Crystal structure of beta-catenin/ICAT helical domain/unphosphorylated APC R3

X-ray diffraction
2.1Å resolution
Source organism: Homo sapiens
Assembly composition:
hetero trimer (preferred)
Entry contents: 3 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero trimer
Accessible surface area: 25062.76 Å2
Buried surface area: 3070.76 Å2
Dissociation area: 634.83 Å2
Dissociation energy (ΔGdiss): -1.5 kcal/mol
Dissociation entropy (TΔSdiss): 10.41 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-150341

Macromolecules

Chain: A
Length: 519 amino acids
Theoretical weight: 56.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P35222 (Residues: 146-664; Coverage: 67%)
Gene names: CTNNB, CTNNB1, OK/SW-cl.35, PRO2286
Pfam: Armadillo/beta-catenin-like repeat
InterPro:
CATH: Leucine-rich Repeat Variant
SCOP: Armadillo repeat

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Chain: B
Length: 46 amino acids
Theoretical weight: 5.24 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9NSA3 (Residues: 8-53; Coverage: 57%)
Gene names: CTNNBIP1, ICAT
Pfam: Beta-catenin-interacting protein ICAT
InterPro:
CATH: Beta-catenin-interacting ICAT
SCOP: beta-catenin-interacting protein ICAT

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Chain: C
Length: 15 amino acids
Theoretical weight: 1.63 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P25054 (Residues: 1484-1498; Coverage: 1%)
Gene names: APC, DP2.5
Pfam: APC repeat

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