1F2H: PDB entry 1F2H

Solution structure of the N-terminal domain of the TNFR1 associated protein, tradd. Determined by solution NMR. Released 30 May 2001.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
1,301
Mol. weight
18.57 kDa
Released
30 May 2001

Explore 1F2H in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 6 helices, 4 β-strands

ElementResiduesLengthSheet
β-strand14-2071
α-helix28-314
α-helix35-5218
β-strand61-6771
β-strand70-7671
α-helix80-10728
β-strand115-11951
α-helix125-1306
α-helix132-14110
α-helix150-16213

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Tumor necrosis factor receptor type 1 associated death domain proteinAprotein169Homo sapiensQ15628 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1F2H_1 TUMOR NECROSIS FACTOR RECEPTOR TYPE 1 ASSOCIATED DEATH DOMAIN PROTEIN (chains A)
MAAGQNGHEEWVGSAYLFVESSLDKVVLSDAYAHPQQKVAVYRALQAALAESGGSPDVLQ
MLKIHRSDPQLIVQLRFCGRQPCGRFLRAYREGALRAALQRSLAAALAQHSVPLQLELRA
GAERLDALLADEERCLSCILAQQPDRLRDEELAELEDALRNLKCGSGAR

Primary citation

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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