Solution structure of the N-terminal domain of the TNFR1 associated protein, tradd. Determined by solution NMR. Released 30 May 2001.
Explore 1F2H in 3D Show helices and sheets RCSB PDB PDBe
1F2H contains 6 α-helices and 4 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 | 14-20 | 7 | 1 |
| α-helix | 28-31 | 4 | |
| α-helix | 35-52 | 18 | |
| β-strand | 61-67 | 7 | 1 |
| β-strand | 70-76 | 7 | 1 |
| α-helix | 80-107 | 28 | |
| β-strand | 115-119 | 5 | 1 |
| α-helix | 125-130 | 6 | |
| α-helix | 132-141 | 10 | |
| α-helix | 150-162 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tumor necrosis factor receptor type 1 associated death domain protein | A | protein | 169 | Homo sapiens | Q15628 (AlphaFold model) |
>1F2H_1 TUMOR NECROSIS FACTOR RECEPTOR TYPE 1 ASSOCIATED DEATH DOMAIN PROTEIN (chains A) MAAGQNGHEEWVGSAYLFVESSLDKVVLSDAYAHPQQKVAVYRALQAALAESGGSPDVLQ MLKIHRSDPQLIVQLRFCGRQPCGRFLRAYREGALRAALQRSLAAALAQHSVPLQLELRA GAERLDALLADEERCLSCILAQQPDRLRDEELAELEDALRNLKCGSGAR
Solution structure of N-TRADD and characterization of the interaction of N-TRADD and C-TRAF2, a key step in the TNFR1 signaling pathway. Tsao, D.H., McDonagh, T., Telliez, J.B. et al. Mol Cell (2000) 5:1051-1057. DOI 10.1016/S1097-2765(00)80270-1 · 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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