Structure of PDB 5vgo Chain A

Receptor sequence
>5vgoA (length=265) Species: 9606 (Homo sapiens) [Search protein sequence]
SWEIDPKDLTFLKELGTGQFGVVKYGKWRGQYDVAIKMIKEGSMSEDEFI
EEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCLLNYLREMRHRF
QTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLS
RYVLDDEYTSSVGSKFPVRWSPPEVLMYSKFSSKSDIWAFGVLMWEIYSL
GKMPYERFTNSETAEHIAQGLRLYRPHLASEKVYTIMYSCWHEKADERPT
FKILLSNILDVMDEN
3D structure
PDB5vgo Discovery of Potent and Selective Tricyclic Inhibitors of Bruton's Tyrosine Kinase with Improved Druglike Properties.
ChainA
Resolution1.621 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 9B1 A L408 G411 F413 V416 K430 M477 A478 G480 N526 L528 D539 Y551 L15 G18 F20 V23 K37 M84 A85 G87 N133 L135 D146 Y158 MOAD: Ki=1.28nM
PDBbind-CN: -logKd/Ki=8.70,IC50=0.002uM
BindingDB: Ki=1.3nM,EC50=33nM,IC50=87nM
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:5vgo, PDBe:5vgo, PDBj:5vgo
PDBsum5vgo
PubMed28626519
UniProtQ06187|BTK_HUMAN Tyrosine-protein kinase BTK (Gene Name=BTK)

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