Structure of PDB 3piy Chain A

Receptor sequence
>3piyA (length=262) Species: 9606 (Homo sapiens) [Search protein sequence]
GYGSWEIDPKDLTFLKELGTGQFGVVKYGKWRGQYDVAIKMIEDEFIEEA
KVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCLLNYLREMRHRFQTQ
QLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYV
LDDEYTSSVGSKFPVRWSPPEVLMYSKFSSKSDIWAFGVLMWEIYSLGKM
PYERFTNSETAEHIAQGLRLYRPHLASEKVYTIMYSCWHEKADERPTFKI
LLSNILDVMDEE
3D structure
PDB3piy Insights into the conformational flexibility of Bruton's tyrosine kinase from multiple ligand complex structures.
ChainA
Resolution2.55 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 A523 R525 N526 D539 F559
Catalytic site (residue number reindexed from 1) D125 A127 R129 N130 D143 F163
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 585 A V416 A428 M477 G480 L528 L542 V546 V26 A38 M81 G84 L132 L146 V150 PDBbind-CN: -logKd/Ki=6.54,IC50=0.29uM
BindingDB: Kd=190nM
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:3piy, PDBe:3piy, PDBj:3piy
PDBsum3piy
PubMed21280133
UniProtQ06187|BTK_HUMAN Tyrosine-protein kinase BTK (Gene Name=BTK)

[Back to BioLiP]