1D4V: Trail-DR5 complex

Crystal structure of trail-DR5 complex. Determined by X-ray diffraction at 2.2 Å resolution. Released 1 Nov 1999.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,396
Mol. weight: 32.06 kDa
Released: 1 Nov 1999

Explore 1D4V in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1D4V contains 7 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.

Chain A: 6 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	81	1	3
α-helix	82	1
β-strand	85-87	3	4
β-strand	94-96	3	4
α-helix	97	1
β-strand	102-103	2	5
β-strand	108	1	3
α-helix	113	1
β-strand	114-115	2	5
α-helix	116-119	4
β-strand	123-127	5	6
β-strand	136-139	4	6
β-strand	143-144	2	7
β-strand	154-155	2	7
α-helix	156-157	2
α-helix	160-161	2
β-strand	165-168	4	8
β-strand	171	1	9
β-strand	174	1	9
β-strand	177-179	3	8

Chain B: 1 helix, 12 β-strands

Element	Residues	Length	Sheet
β-strand	123-127	5	1
β-strand	149-150	2	2
β-strand	163-165	3	1
β-strand	167-170	4	2
β-strand	173-176	4	2
β-strand	180-193	14	1
β-strand	205-213	9	2
β-strand	220-228	9	2
β-strand	237-250	14	1
β-strand	255-260	6	2
α-helix	263-265	3
β-strand	266-267	2	1
β-strand	274-280	7	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Tnf-related apoptosis inducing ligand	B	protein	163	Homo sapiens	P50591 (AlphaFold model)
Death receptor 5	A	protein	117	Homo sapiens	O14763 (AlphaFold model)

Sequence of entity 1 (B), FASTA

>1D4V_1 TNF-RELATED APOPTOSIS INDUCING LIGAND (chains B)
PQRVAAHITGTRGRSNTLSSPNSKNEKALGRKINSWESSRSGHSFLSNLHLRNGELVIHE
KGFYYIYSQTYFRFQEEIKENTKNDKQMVQYIYKYTSYPDPILLMKSARNSCWSKDAEYG
LYSIYQGGIFELKENDRIFVSVTNEHLIDMDHEASFFGAFLVG

Sequence of entity 2 (A), FASTA

>1D4V_2 DEATH RECEPTOR 5 (chains A)
PQQKRSSPSEGLCPPGHHISEDGRDCISCKYGQDYSTHWNDLLFCLRCTRCDSGEVELSP
CTTTRNTVCQCEEGTFREEDSPEMCRKCRTGCPRGMVKVGDCTPWSDIECVHKESGD

Primary citation

Structure of the TRAIL-DR5 complex reveals mechanisms conferring specificity in apoptotic initiation. Mongkolsapaya, J., Grimes, J.M., Chen, N. et al. Nat Struct Biol (1999) 6:1048-1053. DOI 10.1038/14935 · PubMed

Other PDB entries of the same protein (UniProt P50591 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1DG6 1.3 Å, Crystal structure of APO2L/TRAIL
1DU3 2.2 Å, Crystal structure of TRAIL-SDR5
1D0G 2.4 Å, Crystal structure of death receptor 5 (DR5) bound to APO2L/TRAIL
1D2Q 2.8 Å, Crystal structure of human trail
5CIR 3.0 Å, Crystal structure of death receptor 4 (DR4; TNFFRSF10A) bound to TRAIL (TNFSF10)
4N90 3.3 Å, Crystal structure of ternary complex of TRAIL, DR5, and Fab fragment from a DR5 agonist…

Browse structure collections

About this viewer

MolViewer shows 1D4V 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.