A new paradigm for tumor necrosis factor signalling. Determined by X-ray diffraction at 2.25 Å resolution. Released 7 Dec 1995.
Explore 1NCF in 3D Show helices and sheets RCSB PDB PDBe
1NCF contains 21 α-helices and 42 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 |
|---|---|---|---|
| α-helix | 16 | 1 | |
| β-strand | 19-22 | 4 | 1 |
| β-strand | 25-31 | 7 | 1 |
| α-helix | 32 | 1 | |
| β-strand | 33 | 1 | 2 |
| α-helix | 34 | 1 | |
| β-strand | 37-41 | 5 | 3 |
| β-strand | 48 | 1 | 4 |
| α-helix | 49-50 | 2 | |
| β-strand | 51-54 | 4 | 3 |
| α-helix | 55-56 | 2 | |
| β-strand | 59-60 | 2 | 5 |
| β-strand | 65 | 1 | 2 |
| α-helix | 70 | 1 | |
| β-strand | 71-72 | 2 | 5 |
| α-helix | 73-76 | 4 | |
| α-helix | 78-80 | 3 | |
| β-strand | 83-86 | 4 | 6 |
| β-strand | 89 | 1 | 7 |
| β-strand | 92 | 1 | 7 |
| α-helix | 93-94 | 2 | |
| β-strand | 95-97 | 3 | 6 |
| β-strand | 102-106 | 5 | 8 |
| β-strand | 112-116 | 5 | 8 |
| α-helix | 117-118 | 2 | |
| β-strand | 123-127 | 5 | 9 |
| β-strand | 130 | 1 | 10 |
| β-strand | 133 | 1 | 10 |
| β-strand | 136-139 | 4 | 9 |
| α-helix | 140 | 1 | |
| β-strand | 146 | 1 | 11 |
| β-strand | 149 | 1 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 15 | 1 | |
| β-strand | 19-21 | 3 | 12 |
| β-strand | 29-31 | 3 | 12 |
| α-helix | 32 | 1 | |
| β-strand | 33 | 1 | 13 |
| α-helix | 34 | 1 | |
| β-strand | 37-41 | 5 | 14 |
| β-strand | 48 | 1 | 4 |
| α-helix | 49-50 | 2 | |
| β-strand | 51-54 | 4 | 14 |
| α-helix | 55-56 | 2 | |
| β-strand | 59-60 | 2 | 15 |
| β-strand | 65 | 1 | 13 |
| α-helix | 70 | 1 | |
| β-strand | 71-72 | 2 | 15 |
| α-helix | 73-74 | 2 | |
| α-helix | 78-80 | 3 | |
| β-strand | 83-86 | 4 | 16 |
| β-strand | 89 | 1 | 17 |
| β-strand | 92 | 1 | 17 |
| β-strand | 95-97 | 3 | 16 |
| β-strand | 102-106 | 5 | 18 |
| β-strand | 112-116 | 5 | 18 |
| α-helix | 117-119 | 3 | |
| β-strand | 125-127 | 3 | 19 |
| β-strand | 130 | 1 | 20 |
| β-strand | 133 | 1 | 20 |
| α-helix | 134-135 | 2 | |
| β-strand | 136-137 | 2 | 19 |
| β-strand | 143-146 | 4 | 21 |
| β-strand | 149-152 | 4 | 21 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tumor necrosis factor receptor | A, B | protein | 162 | Homo sapiens | P19438 (AlphaFold model) |
>1NCF_1 TUMOR NECROSIS FACTOR RECEPTOR (chains A, B) MDSVCPQGKYIHPQNNSICCTKCHKGTYLYNDCPGPGQDTDCRECESGSFTASENHLRHC LSCSKCRKEMGQVEISSCTVDRDTVCGCRKNQYRHYWSENLFQCFNCSLCLNGTVHLSCQ EKQNTVCTCHAGFFLRENECVSCSNCKKSLECTKLCLPQIEN
Crystallographic evidence for dimerization of unliganded tumor necrosis factor receptor. Naismith, J.H., Devine, T.Q., Brandhuber, B.J. et al. J Biol Chem (1995) 270:13303-13307. DOI 10.1074/jbc.270.22.13303 · PubMed
Other PDB entries of the same protein (UniProt P19438 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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