› 3knv

X-ray diffraction
1.9Å resolution

Crystal structure of the RING and first zinc finger domains of TRAF2

Released:
DOI: 10.2210/pdb3knv/pdb
PDB entry 3knv coloured by chain, front view.
PDB entry 3knv coloured by chain, side view.
PDB entry 3knv coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for the lack of E2 interaction in the RING domain of TRAF2.
Yin Q, Lamothe B, Darnay BG, Wu H
Biochemistry 48 10558-67 (2009)
PMID: 19810754

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:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171446 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
TNF receptor-associated factor 2 Chain: A
Molecule details ›
Chain: A
Length: 141 amino acids
Theoretical weight: 15.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q12933 (Residues: 1-133; Coverage: 27%)
Gene names: TRAF2, TRAP3
Sequence domains:
Structure domains: Zinc/RING finger domain, C3HC4 (zinc finger)

Ligands and Environments

1 bound ligand:
Ligand ZN 3 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P6522
Unit cell:
a: 43.669Å b: 43.669Å c: 284.393Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.216 0.216 0.239
Expression system: Escherichia coli

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Citations

26 review citations

NF-κB, the first quarter-century: remarkable progress and outstanding questions.
Hayden et al. (2012)
25 more

4 mentions without citation

Structural studies of NF-κB signaling.
Zheng et al. (2011)
3 more