› 1oqa

Solution NMR

Solution structure of the BRCT-c domain from human BRCA1

Released:
DOI: 10.2210/pdb1oqa/pdb
PDB entry 1oqa coloured by chain, ensemble of 15 models, front view.
PDB entry 1oqa coloured by chain, ensemble of 15 models, side view.
PDB entry 1oqa coloured by chain, ensemble of 15 models, top view.
Source organism: Homo sapiens
Primary publication:
Solution structure, backbone dynamics, and association behavior of the C-terminal BRCT domain from the breast cancer-associated protein BRCA1.
Gaiser OJ, Ball LJ, Schmieder P, Leitner D, Strauss H, Wahl M, Kühne R, Oschkinat H, Heinemann U
Biochemistry 43 15983-95 (2004)
PMID: 15609993

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:
Cellular component:
  • not assigned
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: A
Molecule details ›
Chain: A
Length: 110 amino acids
Theoretical weight: 12.37 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P38398 (Residues: 1755-1863; Coverage: 6%)
Gene names: BRCA1, RNF53
Sequence domains: BRCA1 C Terminus (BRCT) domain
Structure domains: BRCT domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing, distance geometry
Expression system: Escherichia coli BL21

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Citations

1 review citation

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Cortese et al. (2008)
9 other articles

7 mentions without citation

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