4k8u

X-ray diffraction
2.3Å resolution

Crystal structure of TRAF4 TRAF domain

Released:
Source organism: Homo sapiens
Primary publication:
Structure of the TRAF4 TRAF domain with a coiled-coil domain and its implications for the TRAF4 signalling pathway.
Acta Crystallogr D Biol Crystallogr 70 2-10 (2014)
PMID: 24419373

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
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo trimer (preferred)
PDBe Complex ID:
PDB-CPX-189747 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
TNF receptor-associated factor 4 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 198 amino acids
Theoretical weight: 22.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9BUZ4 (Residues: 281-470; Coverage: 40%)
Gene names: CART1, MLN62, RNF83, TRAF4
Sequence domains: TRAF/meprin, MATH domain
Structure domains: Apoptosis, Tumor Necrosis Factor Receptor Associated Protein 2; Chain A

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 5C (4A)
Spacegroup: P212121
Unit cell:
a: 58.949Å b: 87.989Å c: 117.364Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.24 0.237 0.281
Expression system: Escherichia coli