Crystal structure of death receptor 5 (DR5) bound to APO2L/TRAIL. Determined by X-ray diffraction at 2.4 Å resolution. Released 22 Oct 1999.
Explore 1D0G in 3D Show helices and sheets RCSB PDB PDBe
1D0G contains 23 α-helices and 89 β-strands across 6 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 | 123-127 | 5 | 25 |
| β-strand | 149-150 | 2 | 26 |
| β-strand | 155 | 1 | 25 |
| β-strand | 157 | 1 | 27 |
| β-strand | 162 | 1 | 27 |
| β-strand | 163-165 | 3 | 25 |
| β-strand | 167-170 | 4 | 26 |
| β-strand | 173-176 | 4 | 26 |
| β-strand | 180-192 | 13 | 25 |
| β-strand | 205-213 | 9 | 26 |
| β-strand | 220-228 | 9 | 26 |
| α-helix | 229-230 | 2 | |
| β-strand | 238-250 | 13 | 25 |
| β-strand | 255-260 | 6 | 26 |
| α-helix | 263-265 | 3 | |
| β-strand | 266 | 1 | 25 |
| β-strand | 274-279 | 6 | 25 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 123-128 | 6 | 26 |
| β-strand | 149-150 | 2 | 28 |
| β-strand | 154-155 | 2 | 26 |
| α-helix | 158-160 | 3 | |
| β-strand | 163-165 | 3 | 26 |
| β-strand | 167-170 | 4 | 28 |
| β-strand | 173-176 | 4 | 28 |
| β-strand | 180-192 | 13 | 26 |
| β-strand | 205-213 | 9 | 28 |
| β-strand | 220-228 | 9 | 28 |
| β-strand | 238-250 | 13 | 26 |
| β-strand | 255-260 | 6 | 28 |
| α-helix | 263-265 | 3 | |
| β-strand | 266-267 | 2 | 26 |
| β-strand | 274-279 | 6 | 26 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 24 | 1 | 1 |
| β-strand | 27 | 1 | 1 |
| β-strand | 28 | 1 | 2 |
| β-strand | 32-34 | 3 | 3 |
| β-strand | 41-43 | 3 | 3 |
| α-helix | 44-45 | 2 | |
| β-strand | 49-50 | 2 | 4 |
| β-strand | 55 | 1 | 2 |
| α-helix | 60 | 1 | |
| β-strand | 61-62 | 2 | 4 |
| α-helix | 63-64 | 2 | |
| β-strand | 70-74 | 5 | 5 |
| β-strand | 83-86 | 4 | 5 |
| α-helix | 87 | 1 | |
| β-strand | 90-93 | 4 | 6 |
| β-strand | 96-102 | 7 | 6 |
| α-helix | 103-104 | 2 | |
| β-strand | 112-115 | 4 | 7 |
| β-strand | 118 | 1 | 8 |
| β-strand | 121 | 1 | 8 |
| β-strand | 124-126 | 3 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 24 | 1 | 9 |
| β-strand | 27 | 1 | 9 |
| β-strand | 28 | 1 | 10 |
| β-strand | 32-34 | 3 | 11 |
| β-strand | 41-43 | 3 | 11 |
| α-helix | 44-45 | 2 | |
| β-strand | 49-50 | 2 | 12 |
| β-strand | 55 | 1 | 10 |
| α-helix | 60 | 1 | |
| β-strand | 61-62 | 2 | 12 |
| α-helix | 63-64 | 2 | |
| β-strand | 70-74 | 5 | 13 |
| β-strand | 83-86 | 4 | 13 |
| α-helix | 87 | 1 | |
| β-strand | 90-93 | 4 | 14 |
| β-strand | 96-102 | 7 | 14 |
| α-helix | 103-104 | 2 | |
| α-helix | 107-108 | 2 | |
| β-strand | 111-115 | 5 | 15 |
| β-strand | 118 | 1 | 16 |
| β-strand | 121 | 1 | 16 |
| β-strand | 124-127 | 4 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 24 | 1 | 17 |
| β-strand | 27 | 1 | 17 |
| β-strand | 28 | 1 | 18 |
| β-strand | 32-34 | 3 | 19 |
| β-strand | 41-43 | 3 | 19 |
| α-helix | 44-45 | 2 | |
| β-strand | 49-50 | 2 | 20 |
| β-strand | 55 | 1 | 18 |
| α-helix | 60 | 1 | |
| β-strand | 61-62 | 2 | 20 |
| α-helix | 63-64 | 2 | |
| α-helix | 66-67 | 2 | |
| β-strand | 70-74 | 5 | 21 |
| β-strand | 83-86 | 4 | 21 |
| α-helix | 87 | 1 | |
| β-strand | 90-91 | 2 | 22 |
| β-strand | 101-102 | 2 | 22 |
| α-helix | 103-104 | 2 | |
| β-strand | 111-115 | 5 | 23 |
| β-strand | 118 | 1 | 24 |
| β-strand | 121 | 1 | 24 |
| β-strand | 124-127 | 4 | 23 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Death receptor-5 | R, S, T | protein | 130 | Homo sapiens | O14763 (AlphaFold model) |
| Apoptosis-2 ligand | A, B, D | protein | 168 | Homo sapiens | P50591 (AlphaFold model) |
>1D0G_1 DEATH RECEPTOR-5 (chains R, S, T) ALITQQDLAPQQRAAPQQKRSSPSEGLCPPGHHISEDGRDCISCKYGQDYSTHWNDLLFC LRCTRCDSGEVELSPCTTTRNTVCQCEEGTFREEDSPEMCRKCRTGCPRGMVKVGDCTPW SDIECVHKES
>1D0G_2 APOPTOSIS-2 LIGAND (chains A, B, D) VRERGPQRVAAHITGTRGRSNTLSSPNSKNEKALGRKINSWESSRSGHSFLSNLHLRNGE LVIHEKGFYYIYSQTYFRFQEEIKENTKNDKQMVQYIYKYTSYPDPILLMKSARNSCWSK DAEYGLYSIYQGGIFELKENDRIFVSVTNEHLIDMDHEASFFGAFLVG
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 1 |
Water and common crystallization additives (CL) are not listed.
Triggering cell death: the crystal structure of Apo2L/TRAIL in a complex with death receptor 5. Hymowitz, S.G., Christinger, H.W., Fuh, G. et al. Mol Cell (1999) 4:563-571. DOI 10.1016/S1097-2765(00)80207-5 · PubMed
Other PDB entries of the same protein (UniProt O14763 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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