Structure of PDB 4rx5 Chain A

Receptor sequence
>4rx5A (length=265) Species: 9606 (Homo sapiens) [Search protein sequence]
SWEIDPKDLTFLKELGTGQFGVVKYGKWRGQYDVAIKMIKEGSMSEDEFI
EEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCLLNYLREMRHRF
QTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLS
RYVLDDEYTSSVGSKFPVRWSPPEVLMYSKFSSKSDIWAFGVLMWEIYSL
GKMPYERFTNSETAEHIAQGLRLYRPHLASEKVYTIMYSCWHEKADERPT
FKILLSNILDVMDEN
3D structure
PDB4rx5 Discovery of highly potent and selective Bruton's tyrosine kinase inhibitors: Pyridazinone analogs with improved metabolic stability.
ChainA
Resolution1.356 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 A523 R525 N526 D539 F559
Catalytic site (residue number reindexed from 1) D128 A130 R132 N133 D146 F166
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 3YO A L408 T410 G411 F413 V416 K430 Y476 M477 A478 G480 L528 D539 L15 T17 G18 F20 V23 K37 Y83 M84 A85 G87 L135 D146 MOAD: ic50=3nM
PDBbind-CN: -logKd/Ki=8.52,IC50=3nM
BindingDB: IC50=3.0nM
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:4rx5, PDBe:4rx5, PDBj:4rx5
PDBsum4rx5
PubMed26675441
UniProtQ06187|BTK_HUMAN Tyrosine-protein kinase BTK (Gene Name=BTK)

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