1f3v

X-ray diffraction
2Å resolution

Crystal structure of the complex between the N-terminal domain of TRADD and the TRAF domain of TRAF2

Released:

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
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-171448 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tumor necrosis factor receptor type 1-associated DEATH domain protein Chain: A
Molecule details ›
Chain: A
Length: 179 amino acids
Theoretical weight: 19.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q15628 (Residues: 1-179; Coverage: 57%)
Gene name: TRADD
Sequence domains: TRADD, N-terminal domain
Structure domains: TRADD, N-terminal domain
TNF receptor-associated factor 2 Chain: B
Molecule details ›
Chain: B
Length: 171 amino acids
Theoretical weight: 19.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q12933 (Residues: 331-501; Coverage: 34%)
Gene names: TRAF2, TRAP3
Sequence domains: TRAF/meprin, MATH domain
Structure domains: Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2; Chain A

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: R3
Unit cell:
a: 132.4Å b: 132.4Å c: 62.8Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.229 0.229 0.261
Expression system: Escherichia coli