PDBe 3c5r

X-ray diffraction
2Å resolution

Crystal Structure of the BARD1 Ankyrin Repeat Domain and Its Functional Consequences

Released:

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
Cellular component:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
BRCA1-associated RING domain protein 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 137 amino acids
Theoretical weight: 14.98 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q99728 (Residues: 425-555; Coverage: 17%)
Gene name: BARD1
Sequence domains: Ankyrin repeat
Structure domains: Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 37.847Å b: 74.112Å c: 51.174Å
α: 90° β: 105.23° γ: 90°
R-values:
R R work R free
0.202 0.199 0.268
Expression system: Escherichia coli BL21(DE3)