Structure of PDB 6tfp Chain A

Receptor sequence
>6tfpA (length=266) Species: 9606 (Homo sapiens) [Search protein sequence]
GSWEIDPKDLTFLKELGTGQFGVVKYGKWRGQYDVAIKMIKEGSMSEDEF
IEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCLLNYLREMRHR
FQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGL
SRYVLDDEYTSSVGSKFPVRWSPPEVLMYSKFSSKSDIWAFGVLMWEIYS
LGKMPYERFTNSETAEHIAQGLRLYRPHLASEKVYTIMYSCWHEKADERP
TFKILLSNILDVMDEE
3D structure
PDB6tfp Discovery of LOU064 (Remibrutinib), a Potent and Highly Selective Covalent Inhibitor of Bruton's Tyrosine Kinase.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D521 R525 N526 D539
Catalytic site (residue number reindexed from 1) D129 R133 N134 D147
Enzyme Commision number 2.7.10.2: non-specific protein-tyrosine kinase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 N6Z A L408 G409 G411 Q412 F413 V416 A428 K430 M477 C481 N484 N526 L528 D539 L542 S543 Y551 L16 G17 G19 Q20 F21 V24 A36 K38 M85 C89 N92 N134 L136 D147 L150 S151 Y159 BindingDB: IC50=1300nM
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004713 protein tyrosine kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation

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Molecular Function
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Biological Process
External links
PDB RCSB:6tfp, PDBe:6tfp, PDBj:6tfp
PDBsum6tfp
PubMed32083858
UniProtQ06187|BTK_HUMAN Tyrosine-protein kinase BTK (Gene Name=BTK)

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