Structure of PDB 6tfp Chain D

Receptor sequence
>6tfpD (length=266) Species: 9606 (Homo sapiens) [Search protein sequence]
YGSWEIDPKDLTFLKELGTGQFGVVKYGKWRGQYDVAIKMIKEGSMSEDE
FIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCLLNYLREMRH
RFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFG
LSRYVLDDEYTSSVGSKFPVRWSPPEVLMYSKFSSKSDIWAFGVLMWEIY
SLGKMPYERFTNSETAEHIAQGLRLYRPHLASEKVYTIMYSCWHEKADER
PTFKILLSNILDVMDE
3D structure
PDB6tfp Discovery of LOU064 (Remibrutinib), a Potent and Highly Selective Covalent Inhibitor of Bruton's Tyrosine Kinase.
ChainD
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D521 R525 N526 D539
Catalytic site (residue number reindexed from 1) D130 R134 N135 D148
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 D L408 G409 Q412 F413 V416 A428 K430 M477 C481 N484 L528 D539 S543 Y551 L17 G18 Q21 F22 V25 A37 K39 M86 C90 N93 L137 D148 S152 Y160 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

View graph for
Molecular Function

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

[Back to BioLiP]