PDBe 2r1z

X-ray diffraction
2.1Å resolution

Crystal Structure of the BARD1 BRCT Repeat

Released:
Source organism: Homo sapiens
Entry authors: Lee MS, Edwards RA, Williams RS, Glover MJN

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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
BRCA1-associated RING domain protein 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 209 amino acids
Theoretical weight: 24.05 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q99728 (Residues: 569-777; Coverage: 27%)
Gene name: BARD1
Structure domains: BRCT domain

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: P212121
Unit cell:
a: 56.821Å b: 75.55Å c: 117.967Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.222 0.262
Expression system: Escherichia coli BL21(DE3)