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Crystal structure of trail-DR5 complex

Analyse Crystal structure of trail-DR5 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1D4V
Type: protein
Length: 280 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: TNF-related apoptosis inducing ligand; Death receptor 5
UniProt: P50591
Pockets: 3 · best druggability 0.45

Structure

x-ray diffraction · 2 distinct chains · 1% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	TNF-related apoptosis inducing ligand	protein	163	2% helix, 48% strand	P50591
A	Death receptor 5	protein	117	0% helix, 29% strand	—

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	156	0.45	0.76	30	empty
2	65	0.30	0.75	17	empty
3	83	0.29	0.72	18	empty

Interfaces

1 interface between chains.

B–A · 772 Å² buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 7 disulfide (disulfide).

Compared structures

1D4V · Crystal structure of trail-DR5 complex · the same entry in another collection · chain B against B, TM-score 1.00
P50591 · AlphaFold monomer V2.0 prediction for tumor necrosis factor ligand superfamily member 10… · a predicted model of the same protein · chain B against A, TM-score 0.95

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P50591
Elsewhere: RCSB PDB 1D4V · PDBe 1D4V · UniProt P50591

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