Structure of PDB 2f4j Chain A

Receptor sequence
>2f4jA (length=287) Species: 9606 (Homo sapiens) [Search protein sequence]
GMSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKED
TMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLDY
LRECNRQEVNAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHL
VKVADFGLSRLMTGDTYTAPAGAKFPIKWTAPESLAYNKFSIKSDVWAFG
VLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACW
QWNPSDRPSFAEIHQAFETMFQESSISDEVEKELGKQ
3D structure
PDB2f4j Structure of the kinase domain of an imatinib-resistant Abl mutant in complex with the Aurora kinase inhibitor VX-680.
ChainA
Resolution1.91 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) D137 A139 R141 N142 D155 P176
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 VX6 A G249 Y253 V256 A269 T315 E316 F317 M318 T319 G321 L370 D381 G23 Y27 V30 A43 T89 E90 F91 M92 T93 G95 L144 D155 PDBbind-CN: -logKd/Ki=5.66,IC50=2.2uM
BindingDB: IC50=420nM,Kd=9.4nM,Ki=42nM
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:2f4j, PDBe:2f4j, PDBj:2f4j
PDBsum2f4j
PubMed16424036
UniProtP00519|ABL1_HUMAN Tyrosine-protein kinase ABL1 (Gene Name=ABL1)

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