Structure of PDB 3piz Chain A

Receptor sequence
>3pizA (length=245) Species: 9606 (Homo sapiens) [Search protein sequence]
GYGSWEIDPKDLTFLKELGTGVVKYGKWRGQYDVAIKMISEDEFIEEAKV
MMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCLLNYLREMRHRFQTQQL
LEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLFPVRWS
PPEVLMYSKFSSKSDIWAFGVLMWEIYSLGKMPYERFTNSETAEHIAQGL
RLYRPHLASEKVYTIMYSCWHEKADERPTFKILLSNILDVMDEES
3D structure
PDB3piz Insights into the conformational flexibility of Bruton's tyrosine kinase from multiple ligand complex structures.
ChainA
Resolution2.21 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) D123 A125 R127 N128 D141 F145
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 03C A L408 A428 K430 E445 T474 Y476 M477 G480 L528 L18 A35 K37 E47 T76 Y78 M79 G82 L130 MOAD: ic50=3.5uM
PDBbind-CN: -logKd/Ki=5.46,IC50=3.5uM
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:3piz, PDBe:3piz, PDBj:3piz
PDBsum3piz
PubMed21280133
UniProtQ06187|BTK_HUMAN Tyrosine-protein kinase BTK (Gene Name=BTK)

[Back to BioLiP]