› 1jnx

X-ray diffraction
2.5Å resolution

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

Released:
DOI: 10.2210/pdb1jnx/pdb
PDB entry 1jnx coloured by chain, front view.
PDB entry 1jnx coloured by chain, side view.
PDB entry 1jnx coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the BRCT repeat region from the breast cancer-associated protein BRCA1.
Williams RS, Green R, Glover JN
Nat Struct Biol 8 838-42 (2001)
PMID: 11573086

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:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153627 (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:
Ligand NI 1 x NI
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

Quick links

Citations

26 review citations

Molecular views of recombination proteins and their control.
West SC. (2003)
25 more

45 mentions without citation

BRCT domains: easy as one, two, three.
Leung et al. (2011)
44 more