PDBe 1t2v

X-ray diffraction
3.3Å resolution

Structural basis of phospho-peptide recognition by the BRCT domain of BRCA1, structure with phosphopeptide

Released:
Source organism: Homo sapiens
Primary publication:
Structural basis of phosphopeptide recognition by the BRCT domain of BRCA1.
Nat. Struct. Mol. Biol. 11 519-25 (2004)
PMID: 15133503

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 Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 214 amino acids
Theoretical weight: 24.53 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P38398 (Residues: 1646-1859; Coverage: 12%)
Gene names: BRCA1, RNF53
Sequence domains: BRCA1 C Terminus (BRCT) domain
Structure domains: BRCT domain
BRCTide-7PS Chains: F, G, H, I, J
Molecule details ›
Chains: F, G, H, I, J
Length: 16 amino acids
Theoretical weight: 1.85 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: C2221
Unit cell:
a: 97.117Å b: 138.357Å c: 198.266Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.261 0.258 0.301
Expression systems:
  • Escherichia coli
  • Not provided