Structure of PDB 3pj2 Chain A

Receptor sequence
>3pj2A (length=248) Species: 9606 (Homo sapiens) [Search protein sequence]
GYGSWEIDPKDLTFLKELGTGVVKYGKWRGQYDVAIKMIKEGSMSEDEFI
EEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCLLNYLREMRHRF
QTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFFPV
RWSPPEVLMYSKFSSKSDIWAFGVLMWEIYSLGKMPYERFTNSETAEHIA
QGLRLYRPHLASEKVYTIMYSCWHEKADERPTFKILLSNILDVMDEES
3D structure
PDB3pj2 Insights into the conformational flexibility of Bruton's tyrosine kinase from multiple ligand complex structures.
ChainA
Resolution1.75 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) D128 A130 R132 N133 D146 F148
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 04K A E407 L408 V416 A428 M449 M477 G480 L528 D539 E17 L18 V23 A35 M56 M84 G87 L135 D146 MOAD: ic50=7.2uM
PDBbind-CN: -logKd/Ki=5.14,IC50=7.2uM
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:3pj2, PDBe:3pj2, PDBj:3pj2
PDBsum3pj2
PubMed21280133
UniProtQ06187|BTK_HUMAN Tyrosine-protein kinase BTK (Gene Name=BTK)

[Back to BioLiP]