PDBe 1y98

X-ray diffraction
2.5Å resolution

Structure of the BRCT repeats of BRCA1 bound to a CtIP phosphopeptide.

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

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
CtIP PHOSPHORYLATED PEPTIDE Chain: B
Molecule details ›
Chain: B
Length: 12 amino acids
Theoretical weight: 1.3 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

2 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12B
Spacegroup: P6122
Unit cell:
a: 113.118Å b: 113.118Å c: 121.876Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.234 0.234 0.27
Expression systems:
  • Escherichia coli BL21
  • Not provided