PDBe 1t15

X-ray diffraction
1.85Å resolution

Crystal Structure of the Brca1 BRCT Domains in Complex with the Phosphorylated Interacting Region from Bach1 Helicase

Released:

Function and Biology Details

Reactions catalysed:
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine
ATP + H(2)O = ADP + phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Breast cancer type 1 susceptibility protein Chain: A
Molecule details ›
Chain: A
Length: 214 amino acids
Theoretical weight: 24.53 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P38398 (Residues: 1646-1859; Coverage: 12%)
Gene names: BRCA1, RNF53
Sequence domains: BRCA1 C Terminus (BRCT) domain
Structure domains: BRCT domain
Fanconi anemia group J protein Chain: B
Molecule details ›
Chain: B
Length: 8 amino acids
Theoretical weight: 962 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q9BX63 (Residues: 988-995; Coverage: 1%)
Gene names: BACH1, BRIP1, FANCJ

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3221
Unit cell:
a: 65.837Å b: 65.837Å c: 93.075Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.206 0.206 0.222
Expression systems:
  • Escherichia coli BL21
  • Not provided