PDBe 4u4a

X-ray diffraction
3.51Å resolution

Complex Structure of BRCA1 BRCT with singly phospho Abraxas

Released:
Source organism: Homo sapiens
Entry authors: Badgujar D, Hosur MV, 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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Breast cancer type 1 susceptibility protein Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 214 amino acids
Theoretical weight: 24.53 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P38398 (Residues: 1646-1859; Coverage: 12%)
Gene names: BRCA1, RNF53
Sequence domains: BRCA1 C Terminus (BRCT) domain
Structure domains: BRCT domain
BRCA1-A complex subunit Abraxas 1 Chains: D, E, F
Molecule details ›
Chains: D, E, F
Length: 11 amino acids
Theoretical weight: 1.33 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:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P41212
Unit cell:
a: 187.5Å b: 187.5Å c: 85.35Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.304 0.301 0.362
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided