› 4jlu

X-ray diffraction
3.5Å resolution

Crystal structure of BRCA1 BRCT with doubly phosphorylated Abraxas

Released:
DOI: 10.2210/pdb4jlu/pdb
PDB entry 4jlu coloured by chain, front view.
PDB entry 4jlu coloured by chain, side view.
PDB entry 4jlu coloured by chain, top view.
Source organism: Homo sapiens
Entry authors: Badgujar D, Varma AK

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-153638 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Breast cancer type 1 susceptibility protein Chain: A
Molecule details ›
Chain: A
Length: 211 amino acids
Theoretical weight: 24.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P38398 (Residues: 1649-1859; Coverage: 11%)
Gene names: BRCA1, RNF53
Sequence domains: BRCA1 C Terminus (BRCT) domain
Structure domains: BRCT domain
BRCA1-A complex subunit Abraxas 1 Chain: B
Molecule details ›
Chain: B
Length: 11 amino acids
Theoretical weight: 1.41 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q6UWZ7 (Residues: 399-409; Coverage: 3%)
Gene names: ABRA1, ABRAXAS1, CCDC98, FAM175A, UNQ496/PRO1013

Ligands and Environments

No bound ligands
1 modified residue:
Ligand SEP 2 x SEP

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: P6122
Unit cell:
a: 113.599Å b: 113.599Å c: 121.61Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.3 0.298 0.327
Expression systems:
  • Escherichia coli
  • Not provided

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