GL1X · GenesisL1 explorer

Research workbench

AlphaFold monomer V2.0 prediction for tyrosine-protein kinase btk (P35991)

Analyse AlphaFold monomer V2.0 prediction for tyrosine-protein kinase btk (P35991) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
P35991
Type
protein
Length
659 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x362a6d063b1B7E1B6EfD3A9A7CA3612e3FE037AA
UniProt
P35991

Structure

1 distinct chain.

ChainMoleculeTypeResiduesSecondary structureUniProt
A—protein659—P35991

Compared structures

  • 4XI2 · Crystal Structure of an auto-inhibited form of Bruton's Tryrosine Kinase · an experimental structure of the same protein · chain A against A, TM-score 0.47
  • 4XI2 · Crystal structure of an auto-inhibited form of BRUTON'S tryrosine kinase · an experimental structure of the same protein · chain A against A, TM-score 0.47
  • 8GMB · Crystal structure of the full-length Bruton's tyrosine kinase (PH-TH domain not visible) · an experimental structure of the same protein · chain A against A, TM-score 0.46
  • 8S93 · Crystal structure of the PH-TH/kinase complex of Bruton's tyrosine kinase · an experimental structure of the same protein · chain A against A, TM-score 0.45
  • 8FF0 · Structure of BTK kinase domain with the second-generation inhibitor tirabrutinib · an experimental structure of the same protein · chain A against A, TM-score 0.40
  • 8FD9 · Structure of BTK kinase domain with the second-generation inhibitor acalabrutinib · an experimental structure of the same protein · chain A against A, TM-score 0.40
  • 8S9F · Crystal structure of the kinase domain of Bruton's Tyrosine Kinase bound to dasatinib · an experimental structure of the same protein · chain A against A, TM-score 0.35

Analyse

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