Structure of PDB 4rg0 Chain A

Receptor sequence
>4rg0A (length=263) Species: 9606 (Homo sapiens) [Search protein sequence]
EIDPKDLTFLKELGTGQFGVVKYGKWRGQYDVAIKMIKEGSMSEDEFIEE
AKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCLLNYLREARHAFQT
QQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRY
VLDDEYTSSVGSKFPVRWSPPEVLMYSKFSSKSDIWAFGVLMWEIYSLGK
MPYERFTNSETAEHIAQGLRLYRPHLASAAVYTIMYSCWHEKADERPTFK
ILLSNILDVMDEE
3D structure
PDB4rg0 Finding the perfect spot for fluorine: Improving potency up to 40-fold during a rational fluorine scan of a Bruton's Tyrosine Kinase (BTK) inhibitor scaffold.
ChainA
Resolution2.5 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) D126 A128 R130 N131 D144 F164
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 3P0 A L408 G411 V416 A428 K430 Y476 M477 A478 G480 N526 L528 D539 L13 G16 V21 A33 K35 Y81 M82 A83 G85 N131 L133 D144 MOAD: ic50=50nM
PDBbind-CN: -logKd/Ki=7.30,IC50=50nM
BindingDB: IC50=50nM
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:4rg0, PDBe:4rg0, PDBj:4rg0
PDBsum4rg0
PubMed25466710
UniProtQ06187|BTK_HUMAN Tyrosine-protein kinase BTK (Gene Name=BTK)

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