Structure of PDB 3ik3 Chain B

Receptor sequence
>3ik3B (length=286) Species: 10090 (Mus musculus) [Search protein sequence]
GSPNYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLKEDT
MEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIIIEFMTYGNLLDYL
RECNRQEVSAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLV
KVADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGV
LLWEIATYGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQ
WNPSDRPSFAEIHQAFETMFQESSISDEVEKELGKR
3D structure
PDB3ik3 AP24534, a pan-BCR-ABL inhibitor for chronic myeloid leukemia, potently inhibits the T315I mutant and overcomes mutation-based resistance.
ChainB
Resolution1.9 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) D136 A138 R140 N141 D154 P175
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 0LI B L248 Y253 A269 K271 E286 M290 I293 V299 I313 I315 F317 M318 I360 H361 L370 V379 A380 D381 F382 L21 Y26 A42 K44 E59 M63 I66 V72 I86 I88 F90 M91 I133 H134 L143 V152 A153 D154 F155 MOAD: ic50=2nM
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:3ik3, PDBe:3ik3, PDBj:3ik3
PDBsum3ik3
PubMed19878872
UniProtP00520|ABL1_MOUSE Tyrosine-protein kinase ABL1 (Gene Name=Abl1)

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