Structure of PDB 3ue4 Chain A

Receptor sequence
>3ue4A (length=270) Species: 9606 (Homo sapiens) [Search protein sequence]
DKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVEE
FLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECNR
QEVNAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVADF
GLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEI
ATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPSD
RPSFAEIHQAFETMFQESSI
3D structure
PDB3ue4 Structural and spectroscopic analysis of the kinase inhibitor bosutinib and an isomer of bosutinib binding to the abl tyrosine kinase domain.
ChainA
Resolution2.424 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D363 A365 R367 N368 D381 P402
Catalytic site (residue number reindexed from 1) D131 A133 R135 N136 D149 P170
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 DB8 A L248 A269 K271 V299 I313 T315 F317 M318 T319 L370 F382 L16 A37 K39 V67 I81 T83 F85 M86 T87 L138 F150 PDBbind-CN: -logKd/Ki=8.96,IC50=1.1nM
BindingDB: IC50=1.1nM,Kd=0.057000nM
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

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Molecular Function
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Biological Process
External links
PDB RCSB:3ue4, PDBe:3ue4, PDBj:3ue4
PDBsum3ue4
PubMed22493660
UniProtP00519|ABL1_HUMAN Tyrosine-protein kinase ABL1 (Gene Name=ABL1)

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