› 3k0k

X-ray diffraction
2.7Å resolution

Crystal Structure of BRCA1 BRCT in complex with a minimal recognition tetrapeptide with a free carboxy C-terminus.

Released:
DOI: 10.2210/pdb3k0k/pdb
PDB entry 3k0k coloured by chain, front view.
PDB entry 3k0k coloured by chain, side view.
PDB entry 3k0k coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Comparison of the structures and peptide binding specificities of the BRCT domains of MDC1 and BRCA1.
Campbell SJ, Edwards RA, Glover JN
Structure 18 167-76 (2010)
PMID: 20159462

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 analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153631 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Breast cancer type 1 susceptibility protein Chain: A
Molecule details ›
Chain: A
Length: 215 amino acids
Theoretical weight: 24.66 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
phospho peptide pSPTF-COOH Chain: B
Molecule details ›
Chain: B
Length: 4 amino acids
Theoretical weight: 530 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand NI 1 x NI
Ligand CL 1 x CL
1 modified residue:
Ligand SEP 1 x SEP

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P6122
Unit cell:
a: 114.422Å b: 114.422Å c: 123.005Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.261 0.259 0.299
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

6 review citations

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

5 mentions without citation

Phosphopeptide interactions with BRCA1 BRCT domains: More than just a motif.
Wu et al. (2015)
4 more