PDBe 4ifi

X-ray diffraction
2.2Å resolution

Structure of human BRCA1 BRCT in complex with BAAT peptide

Released:
Source organism: Homo sapiens

Function and Biology Details

Reaction 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
Biochemical function:
Cellular component:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
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
BRCA1-associated ATM activator 1 Chain: B
Molecule details ›
Chain: B
Length: 6 amino acids
Theoretical weight: 773 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q6PJG6 (Residues: 268-273; Coverage: 1%)
Gene names: BAAT1, BRAT1, C7orf27

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P3221
Unit cell:
a: 65.22Å b: 65.22Å c: 91.356Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.2 0.197 0.261
Expression systems:
  • Escherichia coli BL21
  • Not provided