1DU3: TRAIL-SDR5
Crystal structure of TRAIL-SDR5. Determined by X-ray diffraction at 2.2 Å resolution. Released 27 Sept 2000.
- Method
- X-ray diffraction
- Resolution
- 2.2 Å
- Organism
- Homo sapiens
- Chains
- 12
- Atoms
- 12,108
- Mol. weight
- 204.73 kDa
- Ligands
- ZN
- Released
- 27 Sept 2000
Explore 1DU3 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
1DU3 contains 38 α-helices and 177 β-strands across 12 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.
Chain A: 4 helices, 12 β-strands
| 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 | 1 | |
| β-strand | 49-50 | 2 | 4 |
| β-strand | 55 | 1 | 2 |
| α-helix | 60 | 1 | |
| β-strand | 61-62 | 2 | 4 |
| α-helix | 63-66 | 4 | |
| β-strand | 70-74 | 5 | 5 |
| β-strand | 83-86 | 4 | 5 |
| α-helix | 87 | 1 | |
| β-strand | 91-93 | 3 | 6 |
| β-strand | 96-101 | 6 | 6 |
Chain B: 6 helices, 19 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 28 | 1 | 7 |
| β-strand | 32-34 | 3 | 8 |
| β-strand | 41-43 | 3 | 8 |
| α-helix | 44-45 | 2 | |
| β-strand | 49-50 | 2 | 9 |
| β-strand | 55 | 1 | 7 |
| α-helix | 60 | 1 | |
| β-strand | 61-62 | 2 | 9 |
| α-helix | 63 | 1 | |
| β-strand | 64 | 1 | 10 |
| α-helix | 65-66 | 2 | |
| β-strand | 70-74 | 5 | 11 |
| β-strand | 77 | 1 | 12 |
| β-strand | 80 | 1 | 12 |
| β-strand | 83-86 | 4 | 11 |
| α-helix | 87 | 1 | |
| β-strand | 90-91 | 2 | 13 |
| β-strand | 101-102 | 2 | 13 |
| α-helix | 103-104 | 2 | |
| β-strand | 111 | 1 | 14 |
| β-strand | 115 | 1 | 15 |
| β-strand | 118 | 1 | 16 |
| β-strand | 121 | 1 | 16 |
| β-strand | 124 | 1 | 15 |
| β-strand | 127 | 1 | 14 |
Chain C: 3 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 24-26 | 3 | |
| β-strand | 28 | 1 | 17 |
| β-strand | 30 | 1 | 18 |
| β-strand | 32-33 | 2 | 18 |
| β-strand | 42-43 | 2 | 18 |
| α-helix | 44 | 1 | |
| β-strand | 55 | 1 | 17 |
| α-helix | 62-63 | 2 | |
| β-strand | 64 | 1 | 19 |
| β-strand | 70-74 | 5 | 20 |
| β-strand | 77 | 1 | 21 |
| β-strand | 80 | 1 | 21 |
| β-strand | 83-86 | 4 | 20 |
| β-strand | 91 | 1 | 22 |
| β-strand | 101 | 1 | 22 |
| β-strand | 118 | 1 | 23 |
| β-strand | 121 | 1 | 23 |
Chain D: 3 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 123-127 | 5 | 24 |
| β-strand | 128 | 1 | 25 |
| α-helix | 132-134 | 3 | |
| β-strand | 149-150 | 2 | 26 |
| β-strand | 154 | 1 | 25 |
| β-strand | 163-165 | 3 | 24 |
| β-strand | 167-169 | 3 | 26 |
| β-strand | 174-176 | 3 | 26 |
| β-strand | 180-192 | 13 | 24 |
| β-strand | 205-213 | 9 | 26 |
| α-helix | 219 | 1 | |
| β-strand | 220-228 | 9 | 26 |
| β-strand | 238-250 | 13 | 24 |
| β-strand | 255-260 | 6 | 26 |
| α-helix | 263-265 | 3 | |
| β-strand | 266-267 | 2 | 24 |
| β-strand | 274-280 | 7 | 24 |
Chain E: 2 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 123-127 | 5 | 27 |
| β-strand | 128 | 1 | 28 |
| β-strand | 132 | 1 | 10 |
| β-strand | 149-150 | 2 | 29 |
| α-helix | 151 | 1 | |
| β-strand | 154 | 1 | 28 |
| β-strand | 163-165 | 3 | 27 |
| β-strand | 168-169 | 2 | 29 |
| β-strand | 174-175 | 2 | 29 |
| β-strand | 180-192 | 13 | 27 |
| β-strand | 205-213 | 9 | 29 |
| β-strand | 220-228 | 9 | 29 |
| β-strand | 238-250 | 13 | 27 |
| β-strand | 255-260 | 6 | 29 |
| α-helix | 263-265 | 3 | |
| β-strand | 266-267 | 2 | 27 |
| β-strand | 274-279 | 6 | 27 |
Chain F: 1 helix, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 123-127 | 5 | 29 |
| β-strand | 128 | 1 | 30 |
| β-strand | 132 | 1 | 19 |
| β-strand | 149-150 | 2 | 24 |
| β-strand | 154 | 1 | 30 |
| β-strand | 163-165 | 3 | 29 |
| β-strand | 167-169 | 3 | 24 |
| β-strand | 174-176 | 3 | 24 |
| β-strand | 180-192 | 13 | 29 |
| β-strand | 205-214 | 10 | 24 |
| β-strand | 216-228 | 13 | 24 |
| β-strand | 238-250 | 13 | 29 |
| β-strand | 255-260 | 6 | 24 |
| α-helix | 263-265 | 3 | |
| β-strand | 266 | 1 | 29 |
| β-strand | 274-279 | 6 | 29 |
Chain G: 5 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 28 | 1 | 31 |
| α-helix | 29 | 1 | |
| β-strand | 32-34 | 3 | 32 |
| β-strand | 41-43 | 3 | 32 |
| α-helix | 44-45 | 2 | |
| β-strand | 55 | 1 | 31 |
| α-helix | 60-66 | 7 | |
| β-strand | 70-74 | 5 | 33 |
| β-strand | 77 | 1 | 34 |
| β-strand | 80 | 1 | 34 |
| β-strand | 83-86 | 4 | 33 |
| α-helix | 87 | 1 | |
| β-strand | 90-91 | 2 | 35 |
| β-strand | 101-102 | 2 | 35 |
| β-strand | 111-115 | 5 | 36 |
| β-strand | 118 | 1 | 37 |
| β-strand | 121 | 1 | 37 |
| α-helix | 122-123 | 2 | |
| β-strand | 124-127 | 4 | 36 |
Chain H: 4 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 28 | 1 | 38 |
| β-strand | 32-34 | 3 | 39 |
| β-strand | 41-43 | 3 | 39 |
| α-helix | 44-45 | 2 | |
| β-strand | 49-50 | 2 | 40 |
| β-strand | 55 | 1 | 38 |
| α-helix | 60 | 1 | |
| β-strand | 61-62 | 2 | 40 |
| α-helix | 63 | 1 | |
| β-strand | 64 | 1 | 41 |
| β-strand | 70-74 | 5 | 42 |
| β-strand | 77 | 1 | 43 |
| β-strand | 80 | 1 | 43 |
| β-strand | 83-86 | 4 | 42 |
| α-helix | 87 | 1 | |
| β-strand | 91-93 | 3 | 44 |
| β-strand | 96-101 | 6 | 44 |
| β-strand | 118 | 1 | 45 |
| β-strand | 121 | 1 | 45 |
4 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Death receptor 5 | A, B, C, G, H, I | protein | 130 | Homo sapiens | O14763 (AlphaFold model) |
| Tnf-related apoptosis inducing ligand | D, E, F, J, K, L | protein | 168 | Homo sapiens | P50591 (AlphaFold model) |
Sequence of entity 1 (A, B, C, G, H, I), FASTA
>1DU3_1 DEATH RECEPTOR 5 (chains A, B, C, G, H, I)
ALITQQDLAPQQRAAPQQKRSSPSEGLCPPGHHISEDGRDCISCKYGQDYSTHWNDLLFC
LRCTRCDSGEVELSPCTTTRNTVCQCEEGTFREEDSPEMCRKCRTGCPRGMVKVGDCTPW
SDIECVHKES
Sequence of entity 2 (D, E, F, J, K, L), FASTA
>1DU3_2 TNF-RELATED APOPTOSIS INDUCING LIGAND (chains D, E, F, J, K, L)
VRERGPQRVAAHITGTRGRSNTLSSPNSKNEKALGRKINSWESSRSGHSFLSNLHLRNGE
LVIHEKGFYYIYSQTYFRFQEEIKENTKNDKQMVQYIYKYTSYPDPILLMKSARNSCWSK
DAEYGLYSIYQGGIFELKENDRIFVSVTNEHLIDMDHEASFFGAFLVG
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| ZN | Zinc ion | Zn | 2 |
Primary citation
Crystal structure of TRAIL-DR5 complex identifies a critical role of the unique frame insertion in conferring recognition specificity. Cha, S.-S., Sung, B.-J., Kim, Y.A. et al. J Biol Chem (2000) 275:31171-31177. DOI 10.1074/jbc.M004414200 · PubMed
Other PDB entries of the same protein (UniProt O14763 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 3X3F 2.1 Å, TRAIL-R2 Extracellular Region Complexed to a Fab fragment from Human Agonist Antibody…
- 4I9X 2.1 Å, Crystal structure of human cytomegalovirus glycoprotein UL141 targeting the death…
- 1D4V 2.2 Å, Crystal structure of trail-DR5 complex
- 2H9G 2.32 Å, Crystal structure of phage derived Fab BdF1 with human Death Receptor 5 (DR5)
- 1D0G 2.4 Å, Crystal structure of death receptor 5 (DR5) bound to APO2L/TRAIL
- 6T3J 3.05 Å, Dual Epitope Targeting by Anti-DR5 Antibodies
- 4OD2 3.2 Å, Crystal structure of the Fab fragment of an anti-DR5 antibody bound to DR5
- 4N90 3.3 Å, Crystal structure of ternary complex of TRAIL, DR5, and Fab fragment from a DR5 agonist…
- 1ZA3 3.35 Å, The crystal structure of the YSd1 Fab bound to DR5
- 6NHW Structure of the transmembrane domain of the Death Receptor 5 - Dimer of Trimer
- 6NHY Structure of the transmembrane domain of the Death Receptor 5 mutant (G217Y) - Trimer Only
- 8DPX Preligand association structure of DR5
Browse structure collections
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