Structure of PDB 2e2b Chain A

Receptor sequence
>2e2bA (length=270) Species: 9606 (Homo sapiens) [Search protein sequence]
MDPSSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLM
EVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLR
ECNRQEVNAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVK
VADFGLSRLTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEI
ATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPSD
RPSFAEIHQAFETMFQESSI
3D structure
PDB2e2b Structural factors contributing to the Abl/Lyn dual inhibitory activity of 3-substituted benzamide derivatives
ChainA
Resolution2.2 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) D135 A137 R139 N140 D153 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 406 A L248 Y253 A269 K271 E286 V289 M290 L298 I313 T315 F317 M318 I360 H361 V379 A380 D381 F382 L24 Y29 A45 K47 E58 V61 M62 L70 I85 T87 F89 M90 I132 H133 V151 A152 D153 F154 MOAD: ic50=11nM
PDBbind-CN: -logKd/Ki=7.96,IC50=11nM
BindingDB: IC50=4.0nM
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:2e2b, PDBe:2e2b, PDBj:2e2b
PDBsum2e2b
PubMed17376680
UniProtP00519|ABL1_HUMAN Tyrosine-protein kinase ABL1 (Gene Name=ABL1)

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