Structure of PDB 6xe4 Chain A

Receptor sequence
>6xe4A (length=264) Species: 9606 (Homo sapiens) [Search protein sequence]
WEIDPKDLTFLKELGTGQFGVVKYGKWRGQYDVAIKMIKEGSMSEDEFIE
EAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCLLNYLREMRHRFQ
TQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSR
YVLDDEYTSSVGSKFPVRWSPPEVLMYSKFSSKSDIWAFGVLMWEIYSLG
KMPYERFTNSETAEHIAQGLRLYRPHLASEKVYTIMYSCWHEKADERPTF
KILLSNILDVMDEN
3D structure
PDB6xe4 Stereochemical Differences in Fluorocyclopropyl Amides Enable Tuning of Btk Inhibition and Off-Target Activity.
ChainA
Resolution1.6 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) D127 R131 N132 D145
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 V1G A L408 G411 F413 V416 K430 Y476 M477 A478 G480 L528 D539 S543 Y551 L14 G17 F19 V22 K36 Y82 M83 A84 G86 L134 D145 S149 Y157 MOAD: ic50=2.4nM
BindingDB: IC50=2.4nM
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:6xe4, PDBe:6xe4, PDBj:6xe4
PDBsum6xe4
PubMed32832028
UniProtQ06187|BTK_HUMAN Tyrosine-protein kinase BTK (Gene Name=BTK)

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