Photochemically-enhanced binding of small molecules to the tumor necrosis factor receptor-1. Determined by X-ray diffraction at 2.9 Å resolution. Released 12 Oct 2001.
Explore 1FT4 in 3D Show helices and sheets RCSB PDB PDBe
1FT4 contains 19 α-helices and 39 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 | 19-21 | 3 | 1 |
| β-strand | 29-31 | 3 | 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 | 78-80 | 3 | |
| β-strand | 82-86 | 5 | 6 |
| β-strand | 89 | 1 | 7 |
| β-strand | 90 | 1 | 5 |
| β-strand | 92 | 1 | 7 |
| β-strand | 95-98 | 4 | 6 |
| α-helix | 99 | 1 | |
| β-strand | 102-105 | 4 | 8 |
| β-strand | 109 | 1 | 9 |
| β-strand | 111 | 1 | 9 |
| β-strand | 113-116 | 4 | 8 |
| α-helix | 117-118 | 2 | |
| β-strand | 123-127 | 5 | 10 |
| β-strand | 136-139 | 4 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 19-21 | 3 | 11 |
| β-strand | 29-31 | 3 | 11 |
| α-helix | 32 | 1 | |
| β-strand | 37-41 | 5 | 12 |
| β-strand | 48 | 1 | 4 |
| α-helix | 49-50 | 2 | |
| β-strand | 51-54 | 4 | 12 |
| α-helix | 55-56 | 2 | |
| β-strand | 59-60 | 2 | 13 |
| α-helix | 70 | 1 | |
| β-strand | 71-72 | 2 | 13 |
| α-helix | 73-76 | 4 | |
| α-helix | 78-80 | 3 | |
| β-strand | 83-86 | 4 | 14 |
| β-strand | 89 | 1 | 15 |
| β-strand | 90 | 1 | 13 |
| β-strand | 92 | 1 | 15 |
| β-strand | 95-97 | 3 | 14 |
| α-helix | 99-101 | 3 | |
| β-strand | 103-105 | 3 | 16 |
| β-strand | 113-115 | 3 | 16 |
| α-helix | 116-120 | 5 | |
| β-strand | 121 | 1 | 17 |
| β-strand | 123-125 | 3 | 18 |
| α-helix | 128-129 | 2 | |
| β-strand | 137-139 | 3 | 18 |
| α-helix | 140-142 | 3 | |
| α-helix | 143 | 1 | |
| β-strand | 144-146 | 3 | 17 |
| β-strand | 149-151 | 3 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Soluble tumor necrosis factor receptor 1 | A, B | protein | 162 | Homo sapiens | P19438 (AlphaFold model) |
>1FT4_1 SOLUBLE TUMOR NECROSIS FACTOR RECEPTOR 1 (chains A, B) MDSVCPQGKYIHPQNNSICCTKCHKGTYLYNDCPGPGQDTDCRECESGSFTASENHLRHC LSCSKCRKEMGQVEISSCTVDRDTVCGCRKNQYRHYWSENLFQCFNCSLCLNGTVHLSCQ EKQNTVCTCHAGFFLRENECVSCSNCKKSLECTKLCLPQIEN
| ID | Name | Formula | Copies |
|---|---|---|---|
| 703 | 5-(3-morpholin-4-yl-propyl)-2-(3-nitro-phenyl)-4-thioxo-4,5-dihydro-1-thia-3B,5… | C21 H20 N4 O4 S2 | 1 |
Photochemically enhanced binding of small molecules to the tumor necrosis factor receptor-1 inhibits the binding of TNF-alpha. Carter, P.H., Scherle, P.A., Muckelbauer, J.K. et al. Proc Natl Acad Sci U S A (2001) 98:11879-11884. DOI 10.1073/pnas.211178398 · PubMed
Other PDB entries of the same protein (UniProt P19438 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 1FT4 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.