PDBe 1jnx

X-ray diffraction
2.5Å resolution

Crystal structure of the BRCT repeat region from the breast cancer associated protein, BRCA1

Released:
Source organism: Homo sapiens

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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Breast cancer type 1 susceptibility protein Chain: X
Molecule details ›
Chain: X
Length: 214 amino acids
Theoretical weight: 24.53 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P38398 (Residues: 1646-1859; Coverage: 12%)
Gene names: BRCA1, RNF53
Sequence domains: BRCA1 C Terminus (BRCT) domain
Structure domains: BRCT domain

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P6122
Unit cell:
a: 114.844Å b: 114.844Å c: 122.111Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.262 0.259 0.302
Expression system: Escherichia coli