PDBe 1n5o

X-ray diffraction
2.8Å resolution

Structural consequences of a cancer-causing BRCA1-BRCT missense mutation

Released:
Source organism: Homo sapiens
Primary publication:
Structural consequences of a cancer-causing BRCA1-BRCT missense mutation.
J. Biol. Chem. 278 2630-5 (2003)
PMID: 12427738

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: 24.56 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

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P6122
Unit cell:
a: 114.535Å b: 114.535Å c: 121.527Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.275 0.274 0.298
Expression system: Escherichia coli