PDBe 1t2u

X-ray diffraction
2.8Å resolution

Structural basis of phosphopeptide recognition by the BRCT domain of BRCA1: structure of BRCA1 missense variant V1809F

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

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Breast cancer type 1 susceptibility protein Chain: A
Molecule details ›
Chain: A
Length: 214 amino acids
Theoretical weight: 24.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P38398 (Residues: 1646-1859; Coverage: 12%)
  • Best match: P38398-6 (Residues: 542-673)
Gene names: BRCA1, RNF53
Sequence domains: BRCA1 C Terminus (BRCT) domain
Structure domains: BRCT domain

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: P6122
Unit cell:
a: 113.924Å b: 113.924Å c: 120.906Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.277 0.275 0.294
Expression system: Escherichia coli