PDBe 1jm7

Solution NMR

Solution structure of the BRCA1/BARD1 RING-domain heterodimer

Released:
Source organism: Homo sapiens
Primary publication:
Structure of a BRCA1-BARD1 heterodimeric RING-RING complex.
Nat. Struct. Biol. 8 833-7 (2001)
PMID: 11573085

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:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
BRCA1-associated RING domain protein 1 Chain: B
Molecule details ›
Chain: B
Length: 117 amino acids
Theoretical weight: 13.17 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q99728 (Residues: 26-140; Coverage: 15%)
Gene name: BARD1
Sequence domains: zf-RING of BARD1-type protein
Structure domains: Zinc/RING finger domain, C3HC4 (zinc finger)
Breast cancer type 1 susceptibility protein Chain: A
Molecule details ›
Chain: A
Length: 112 amino acids
Theoretical weight: 12.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P38398 (Residues: 1-110; Coverage: 6%)
Gene names: BRCA1, RNF53
Sequence domains: Zinc finger, C3HC4 type (RING finger)
Structure domains: Zinc/RING finger domain, C3HC4 (zinc finger)

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry simulated annealing
Expression system: Escherichia coli BL21(DE3)