Structure of PDB 2gqg Chain A

Receptor sequence
>2gqgA (length=278) Species: 9606 (Homo sapiens) [Search protein sequence]
GAMDPSSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKT
LKEDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGN
LLDYLRECNRQEVNAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVG
ENHLVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDV
WAFGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELM
RACWQWNPSDRPSFAEIHQAFETMFQES
3D structure
PDB2gqg The Structure of Dasatinib (BMS-354825) Bound to Activated ABL Kinase Domain Elucidates Its Inhibitory Activity against Imatinib-Resistant ABL Mutants
ChainA
Resolution2.4 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) D141 A143 R145 N146 D159 P180
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 1N1 A L248 A269 K271 E286 M290 V299 I313 T315 F317 M318 T319 Y320 G321 L370 L26 A47 K49 E64 M68 V77 I91 T93 F95 M96 T97 Y98 G99 L148 BindingDB: IC50=3.1nM,Kd=1.2nM,EC50=0.040000nM
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:2gqg, PDBe:2gqg, PDBj:2gqg
PDBsum2gqg
PubMed16740718
UniProtP00519|ABL1_HUMAN Tyrosine-protein kinase ABL1 (Gene Name=ABL1)

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