GL1X · GenesisL1 explorer

Research workbench

PH domain and btk motif from BRUTON'S tyrosine kinase mutant R28C

Analyse PH domain and btk motif from BRUTON'S tyrosine kinase mutant R28C in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1BTK
Type
protein
Length
329 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
BRUTON'S tyrosine kinase
EC
2.7.1.112
UniProt
Q06187
Ligands
ZN, NA
Pockets
5 · best druggability 0.42

Structure

x-ray diffraction · 2 distinct chains · 15% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABRUTON'S tyrosine kinase (EC 2.7.1.112)protein16016% helix, 38% strandQ06187
BBRUTON'S tyrosine kinase (EC 2.7.1.112)protein16915% helix, 36% strandQ06187

Ligands and binding sites

  • ZN · Zinc ion · metal · 2 copies · chains A, B
  • NA · Sodium ion · metal · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1690.420.8120empty
2740.420.8020empty
31370.410.7529empty
4610.410.8119empty
5570.290.7512empty

Interfaces

1 interface between chains.

  • A–B · 1087 Ų buried · 14 hydrogen bonds · protein-protein

Compared structures

  • 1BTK · PH domain and btk motif from BRUTON'S tyrosine kinase mutant R28C · 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 0.96

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.