Crystal structure of human trail. Determined by X-ray diffraction at 2.8 Å resolution. Released 11 Feb 2000.
Explore 1D2Q in 3D Show helices and sheets RCSB PDB PDBe
1D2Q contains 4 α-helices and 26 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 | 123-128 | 6 | 1 |
| α-helix | 129 | 1 | |
| β-strand | 149-150 | 2 | 2 |
| β-strand | 154-155 | 2 | 1 |
| β-strand | 163-165 | 3 | 1 |
| β-strand | 167-170 | 4 | 2 |
| β-strand | 173-176 | 4 | 2 |
| β-strand | 180-190 | 11 | 1 |
| β-strand | 206-213 | 8 | 2 |
| α-helix | 219 | 1 | |
| β-strand | 220-227 | 8 | 2 |
| β-strand | 240-250 | 11 | 1 |
| β-strand | 255-260 | 6 | 2 |
| β-strand | 266-267 | 2 | 1 |
| β-strand | 274-280 | 7 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tnf-related apoptosis inducing ligand | A, B | protein | 168 | Homo sapiens | P50591 (AlphaFold model) |
>1D2Q_1 TNF-RELATED APOPTOSIS INDUCING LIGAND (chains A, B) VRERGPQRVAAHITGTRGRSNTLSSPNSKNEKALGRKINSWESSRSGHSFLSNLHLRNGE LVIHEKGFYYIYSQTYFRFQEEIKENTKNDKQMVQYIYKYTSYPDPILLMKSARNSCWSK DAEYGLYSIYQGGIFELKENDRIFVSVTNEHLIDMDHEASFFGAFLVG
2.8 A resolution crystal structure of human TRAIL, a cytokine with selective antitumor activity. Cha, S.S., Kim, M.S., Choi, Y.H. et al. Immunity (1999) 11:253-261. DOI 10.1016/S1074-7613(00)80100-4 · PubMed
Other PDB entries of the same protein (UniProt P50591 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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