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Crystal structure of human trail

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

PDB: 1D2Q
Type: protein
Length: 268 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: TNF-related apoptosis inducing ligand
UniProt: P50591
Pockets: 1 · best druggability 0.42

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	TNF-related apoptosis inducing ligand	protein	134	0% helix, 55% strand	P50591

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	140	0.42	0.75	22	empty

Interfaces

1 interface between chains.

A–B · 82 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

1D2Q · Crystal structure of human trail · the same entry in another collection · chain A against A, 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 A against A, TM-score 0.92

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 1D2Q · PDBe 1D2Q · UniProt P50591

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