Structure of PDB 1m52 Chain A

Receptor sequence
>1m52A (length=271) Species: 10090 (Mus musculus) [Search protein sequence]
YDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDTMEVE
EFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECN
RQEVSAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVAD
FGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWE
IATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPS
DRPSFAEIHQAFETMFQESSI
3D structure
PDB1m52 Crystal Structures of the Kinase Domain of c-Abl in Complex with the Small Molecule Inhibitors PD173955 and Imatinib (STI-571)
ChainA
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D363 A365 R367 N368 D381 P402
Catalytic site (residue number reindexed from 1) D132 A134 R136 N137 D150 P171
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 P17 A G249 Y253 V256 A269 K271 M290 T315 M318 G321 L370 A380 F382 G18 Y22 V25 A38 K40 M59 T84 M87 G90 L139 A149 F151
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:1m52, PDBe:1m52, PDBj:1m52
PDBsum1m52
PubMed12154025
UniProtP00520|ABL1_MOUSE Tyrosine-protein kinase ABL1 (Gene Name=Abl1)

[Back to BioLiP]