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

ElementResiduesLengthSheet
β-strand2411
β-strand2711
β-strand2812
β-strand32-3433
β-strand41-4333
α-helix441
β-strand49-5024
β-strand5512
α-helix601
β-strand61-6224
α-helix63-664
β-strand70-7455
β-strand83-8645
α-helix871
β-strand91-9336
β-strand96-10166
Chain B: 6 helices, 19 β-strands
ElementResiduesLengthSheet
β-strand2817
β-strand32-3438
β-strand41-4338
α-helix44-452
β-strand49-5029
β-strand5517
α-helix601
β-strand61-6229
α-helix631
β-strand64110
α-helix65-662
β-strand70-74511
β-strand77112
β-strand80112
β-strand83-86411
α-helix871
β-strand90-91213
β-strand101-102213
α-helix103-1042
β-strand111114
β-strand115115
β-strand118116
β-strand121116
β-strand124115
β-strand127114
Chain C: 3 helices, 14 β-strands
ElementResiduesLengthSheet
α-helix24-263
β-strand28117
β-strand30118
β-strand32-33218
β-strand42-43218
α-helix441
β-strand55117
α-helix62-632
β-strand64119
β-strand70-74520
β-strand77121
β-strand80121
β-strand83-86420
β-strand91122
β-strand101122
β-strand118123
β-strand121123
Chain D: 3 helices, 14 β-strands
ElementResiduesLengthSheet
β-strand123-127524
β-strand128125
α-helix132-1343
β-strand149-150226
β-strand154125
β-strand163-165324
β-strand167-169326
β-strand174-176326
β-strand180-1921324
β-strand205-213926
α-helix2191
β-strand220-228926
β-strand238-2501324
β-strand255-260626
α-helix263-2653
β-strand266-267224
β-strand274-280724
Chain E: 2 helices, 15 β-strands
ElementResiduesLengthSheet
β-strand123-127527
β-strand128128
β-strand132110
β-strand149-150229
α-helix1511
β-strand154128
β-strand163-165327
β-strand168-169229
β-strand174-175229
β-strand180-1921327
β-strand205-213929
β-strand220-228929
β-strand238-2501327
β-strand255-260629
α-helix263-2653
β-strand266-267227
β-strand274-279627
Chain F: 1 helix, 15 β-strands
ElementResiduesLengthSheet
β-strand123-127529
β-strand128130
β-strand132119
β-strand149-150224
β-strand154130
β-strand163-165329
β-strand167-169324
β-strand174-176324
β-strand180-1921329
β-strand205-2141024
β-strand216-2281324
β-strand238-2501329
β-strand255-260624
α-helix263-2653
β-strand266129
β-strand274-279629
Chain G: 5 helices, 14 β-strands
ElementResiduesLengthSheet
β-strand28131
α-helix291
β-strand32-34332
β-strand41-43332
α-helix44-452
β-strand55131
α-helix60-667
β-strand70-74533
β-strand77134
β-strand80134
β-strand83-86433
α-helix871
β-strand90-91235
β-strand101-102235
β-strand111-115536
β-strand118137
β-strand121137
α-helix122-1232
β-strand124-127436
Chain H: 4 helices, 15 β-strands
ElementResiduesLengthSheet
β-strand28138
β-strand32-34339
β-strand41-43339
α-helix44-452
β-strand49-50240
β-strand55138
α-helix601
β-strand61-62240
α-helix631
β-strand64141
β-strand70-74542
β-strand77143
β-strand80143
β-strand83-86442
α-helix871
β-strand91-93344
β-strand96-101644
β-strand118145
β-strand121145

4 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Death receptor 5A, B, C, G, H, Iprotein130Homo sapiensO14763 (AlphaFold model)
Tnf-related apoptosis inducing ligandD, E, F, J, K, Lprotein168Homo sapiensP50591 (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

IDNameFormulaCopies
ZNZinc ionZn2

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:

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