Structure of PDB 1iep Chain A

Receptor sequence
>1iepA (length=274) Species: 10090 (Mus musculus) [Search protein sequence]
MDPSSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLK
EDTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLL
DYLRECNRQEVSAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGEN
HLVKVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWA
FGVLLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRA
CWQWNPSDRPSFAEIHQAFETMFQ
3D structure
PDB1iep Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571)
ChainA
Resolution2.1 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) D139 A141 R143 N144 D157 P178
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 STI A L248 Y253 A269 K271 E286 M290 V299 I313 T315 F317 M318 I360 H361 R362 A380 D381 F382 L24 Y29 A45 K47 E62 M66 V75 I89 T91 F93 M94 I136 H137 R138 A156 D157 F158 MOAD: ic50=100nM
PDBbind-CN: -logKd/Ki=7.00,IC50=100nM
BindingDB: IC50=10.8nM
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:1iep, PDBe:1iep, PDBj:1iep
PDBsum1iep
PubMed12154025
UniProtP00520|ABL1_MOUSE Tyrosine-protein kinase ABL1 (Gene Name=Abl1)

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