Crystal structure of the complex between the N-terminal domain of TRADD and the TRAF domain of TRAF2. Determined by X-ray diffraction at 2.0 Å resolution. Released 6 Sept 2000.
Explore 1F3V in 3D Show helices and sheets RCSB PDB PDBe
1F3V contains 16 α-helices and 18 β-strands across 2 chains. 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 | 12-21 | 10 | 1 |
| α-helix | 28-33 | 6 | |
| α-helix | 38-48 | 11 | |
| α-helix | 49-53 | 5 | |
| β-strand | 59-66 | 8 | 1 |
| β-strand | 71-78 | 8 | 1 |
| α-helix | 80-91 | 12 | |
| α-helix | 94-106 | 13 | |
| β-strand | 114-120 | 7 | 1 |
| β-strand | 123-124 | 2 | 1 |
| α-helix | 125-128 | 4 | |
| α-helix | 132-141 | 10 | |
| β-strand | 146 | 1 | 2 |
| α-helix | 150-162 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 332-347 | 16 | |
| β-strand | 353-359 | 7 | 3 |
| α-helix | 361-369 | 9 | |
| β-strand | 376-377 | 2 | 4 |
| α-helix | 378-380 | 3 | |
| β-strand | 381-382 | 2 | 4 |
| β-strand | 389-395 | 7 | 4 |
| α-helix | 400-402 | 3 | |
| β-strand | 406-414 | 9 | 4 |
| α-helix | 419-421 | 3 | |
| β-strand | 430-434 | 5 | 3 |
| β-strand | 443-447 | 5 | 3 |
| β-strand | 449 | 1 | 2 |
| α-helix | 454-456 | 3 | |
| α-helix | 458-459 | 2 | |
| β-strand | 463 | 1 | 4 |
| β-strand | 467-474 | 8 | 4 |
| α-helix | 475-478 | 4 | |
| β-strand | 486 | 1 | 3 |
| β-strand | 489-496 | 8 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tumor necrosis factor receptor type 1 associated death domain protein | A | protein | 179 | Homo sapiens | Q15628 (AlphaFold model) |
| Tumor necrosis factor receptor-associated protein | B | protein | 171 | Homo sapiens | Q12933 (AlphaFold model) |
>1F3V_1 TUMOR NECROSIS FACTOR RECEPTOR TYPE 1 ASSOCIATED DEATH DOMAIN PROTEIN (chains A) MAAGQNGHEEWVGSAYLFVESSLDKVVLSDAYAHPQQKVAVYRALQAALAESGGSPDVLQ MLKIHRSDPQLIVQLRFCGRQPCGRFLRAYREGALRAALQRSLAAALAQHSVPLQLELRA GAERLDALLADEERCLSCILAQQPDRLRDEELAELEDALRNLKCGSGARGGDGEVASAP
>1F3V_2 TUMOR NECROSIS FACTOR RECEPTOR-ASSOCIATED PROTEIN (chains B) KDLAMADLEQKVLEMEASTYDGVFIWKISDFPRKRQEAVAGRIPAIFSPAFYTSRYGYKM CLRIYLNGDGTGRGTHLSLFFVVMKGPNDALLRWPFNQKVTLMLLDQNNREHVIDAFRPD VTSSSFQRPVNDMNIASGCPLFCPVSKMEAKNSYVRDDAIFIKAIVDLTGL
A novel mechanism of TRAF signaling revealed by structural and functional analyses of the TRADD-TRAF2 interaction. Park, Y.C., Ye, H., Hsia, C. et al. Cell (2000) 101:777-787. DOI 10.1016/S0092-8674(00)80889-2 · PubMed
Other PDB entries of the same protein (UniProt Q15628 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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