4igk

X-ray diffraction
1.75Å resolution

Structure of human BRCA1 BRCT in complex with ATRIP peptide

Released:
Source organism: Homo sapiens
Primary publication:
Structural basis for the BRCA1 BRCT interaction with the proteins ATRIP and BAAT1.
Biochemistry 52 7618-27 (2013)
PMID: 24073851

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:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-153639 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Breast cancer type 1 susceptibility protein Chains: A, B
Molecule details ›
Chains: A, B
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
ATR-interacting protein Chains: C, D
Molecule details ›
Chains: C, D
Length: 7 amino acids
Theoretical weight: 789 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q8WXE1 (Residues: 237-243; Coverage: 1%)
Gene names: AGS1, ATRIP

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P2
Unit cell:
a: 65.666Å b: 50.309Å c: 73.977Å
α: 90° β: 116.03° γ: 90°
R-values:
R R work R free
0.223 0.159 0.204
Expression systems:
  • Escherichia coli BL21
  • Not provided