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Crystal structure of arq 531 in complex with the kinase domain of btk

Analyse Crystal structure of arq 531 in complex with the kinase domain of btk in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6E4F
Type
protein
Length
270 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tyrosine-protein kinase btk
EC
2.7.10.2
UniProt
Q06187
Ligands
HRA
Pockets
2 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATyrosine-protein kinase btk (EC 2.7.10.2)protein27042% helix, 17% strandQ06187

Ligands and binding sites

  • HRA · 1,5-anhydro-2-{[5-(2-chloro-4-phenoxybenzene-1-carbonyl)-7H-pyrrolo[2,3-d]pyrimidin-4-yl]amino}-2,3, 4-trideoxy-D-erythro-hexitol · ligand · chains A
  • IMD · Imidazole · additive · 2 copies · chains A
  • EDO · 1,2-ethanediol · additive · 2 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16030.740.8167HRA
2860.380.7618EDO

Compared structures

  • 6E4F · Crystal structure of ARQ 531 in complex with the kinase domain of BTK · the same entry in another collection · chain A against A, TM-score 1.00
  • Q06187 · AlphaFold monomer V2.0 prediction for tyrosine-protein kinase btk (Q06187) · a predicted model of the same protein · chain A against A, TM-score 0.97

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