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Crystal structure of human BET3

Analyse Crystal structure of human BET3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1SZ7
Type
protein
Length
159 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Trafficking protein particle complex subunit 3
UniProt
O43617
Ligands
PLM
Pockets
1 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATrafficking protein particle complex subunit 3protein15949% helix, 18% strandO43617

Ligands and binding sites

  • PLM · Palmitic acid · ligand · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12370.760.8930PLM

Modifications

Observed in the structure: 1 lipid (palmitoylation).

Compared structures

  • 1SZ7 · Crystal structure of Human Bet3 · the same entry in another collection · chain A against A, TM-score 1.00
  • O43617 · AlphaFold monomer V2.0 prediction for trafficking protein particle complex subunit 3… · a predicted model of the same protein · chain A against A, TM-score 0.97

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