PDBe 2nte

X-ray diffraction
1.9Å resolution

Crystal Structure of the BARD1 BRCT Domains

Released:
Source organism: Homo sapiens
Primary publication:
Crystal structure of the BARD1 BRCT domains.
Biochemistry 46 7706-12 (2007)
PMID: 17550235

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

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
BRCA1-associated RING domain protein 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 210 amino acids
Theoretical weight: 24.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q99728 (Residues: 568-777; Coverage: 27%)
Gene name: BARD1
Structure domains: Rossmann fold

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12B
Spacegroup: P212121
Unit cell:
a: 57.441Å b: 75.797Å c: 116.57Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.196 0.247
Expression system: Escherichia coli BL21