Structure analysis

Crystal structure of the BRCA1 BRCT repeats bound to a phosphorylated BACH1 peptide

X-ray diffraction
2.3Å resolution
Source organism: Homo sapiens
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: 11250.07 Å2
Buried surface area: 1538.4 Å2
Dissociation area: 769.2 Å2
Dissociation energy (ΔGdiss): 4.39 kcal/mol
Dissociation entropy (TΔSdiss): 8.04 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-153641

Macromolecules

Chain: A
Length: 214 amino acids
Theoretical weight: 24.53 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P38398 (Residues: 1646-1859; Coverage: 12%)
Gene names: BRCA1, RNF53
Pfam: BRCA1 C Terminus (BRCT) domain
InterPro:
CATH: BRCT domain
SCOP: BRCT domain

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Chain: B
Length: 14 amino acids
Theoretical weight: 1.68 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q9BX63 (Residues: 985-998; Coverage: 1%)
Gene names: BACH1, BRIP1, FANCJ

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