Structure of PDB 3mss Chain D

Receptor sequence
>3mssD (length=264) Species: 10090 (Mus musculus) [Search protein sequence]
MDPSYDKWEMERTDITMKHKLGGGQYGEVYEGVWKKYSLTVAVKTLVEEF
LKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMTYGNLLDYLRECNRQ
EVSAVVLLYMATQISSAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFG
LSRLMGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIAT
YGMSPYPGIDLSQVYELLEKDYRMERPEGCPEKVYELMRACWQWNPSDRP
SFAEIHQAFETMFQ
3D structure
PDB3mss Binding or bending: distinction of allosteric Abl kinase agonists from antagonists by an NMR-based conformational assay.
ChainD
Resolution1.95 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) D130 A132 R134 N135 D148 P168
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 D L248 Y253 A269 K271 E286 M290 I313 T315 F317 M318 I360 H361 L370 A380 D381 F382 L21 Y26 A42 K44 E53 M57 I80 T82 F84 M85 I127 H128 L137 A147 D148 F149 BindingDB: IC50=10.8nM
BS02 MS7 D L341 A433 P465 V468 L108 A199 P231 V234
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:3mss, PDBe:3mss, PDBj:3mss
PDBsum3mss
PubMed20450175
UniProtP00520|ABL1_MOUSE Tyrosine-protein kinase ABL1 (Gene Name=Abl1)

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