Crystal structure of the RING and first zinc finger domains of TRAF2. Determined by X-ray diffraction at 1.9 Å resolution. Released 24 Nov 2009.
Explore 3KNV in 3D Show helices and sheets RCSB PDB PDBe
3KNV contains 12 α-helices and 10 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 19 | 1 | 1 |
| α-helix | 20 | 1 | |
| α-helix | 21-23 | 3 | |
| α-helix | 25-27 | 3 | |
| α-helix | 30-32 | 3 | |
| β-strand | 33 | 1 | 1 |
| β-strand | 40 | 1 | 1 |
| β-strand | 44-46 | 3 | 2 |
| β-strand | 52-54 | 3 | 2 |
| α-helix | 55-61 | 7 | |
| α-helix | 62-64 | 3 | |
| β-strand | 67-68 | 2 | 3 |
| α-helix | 70-74 | 5 | |
| β-strand | 84-85 | 2 | 3 |
| α-helix | 87-89 | 3 | |
| β-strand | 91-92 | 2 | 2 |
| α-helix | 94-101 | 8 | |
| β-strand | 104-106 | 3 | 4 |
| β-strand | 115-117 | 3 | 4 |
| α-helix | 118-120 | 3 | |
| α-helix | 121-125 | 5 | |
| α-helix | 130-133 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| TNF receptor-associated factor 2 | A | protein | 141 | Homo sapiens | Q12933 (AlphaFold model) |
>3KNV_1 TNF receptor-associated factor 2 (chains A) MAAASVTPPGSLELLQPGFSKTLLGTKLEAKYLCSACRNVLRRPFQAQCGHRYCSFCLAS ILSSGPQNCAACVHEGIYEEGISILESSSAFPDNAARREVESLPAVCPSDGCTWKGTLKE YESCHEGRCPLMLLEHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 3 |
Structural basis for the lack of E2 interaction in the RING domain of TRAF2. Yin, Q., Lamothe, B., Darnay, B.G. et al. Biochemistry (2009) 48:10558-10567. DOI 10.1021/bi901462e · PubMed
Other PDB entries of the same protein (UniProt Q12933 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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