3fa2

X-ray diffraction
2.2Å resolution

Crystal Structure of the BRCA1 Associated Ring Domain (BARD1) Tandem BRCT Domains

Released:
Source organism: Homo sapiens
Entry authors: Fox III D, Le Trong I, Stenkamp RE, Klevit RE

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

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-189258 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
BRCA1-associated RING domain protein 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 218 amino acids
Theoretical weight: 25.01 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q99728 (Residues: 566-777; Coverage: 27%)
Gene name: BARD1
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: RIGAKU
Spacegroup: P21
Unit cell:
a: 44.979Å b: 67.466Å c: 86.783Å
α: 90° β: 99.2° γ: 90°
R-values:
R R work R free
0.226 0.222 0.298
Expression system: Escherichia coli