Structure of PDB 4e1z Chain A

Receptor sequence
>4e1zA (length=288) Species: 10090 (Mus musculus) [Search protein sequence]
SDPTVFHKRYLKKIRDLGEGHFGKVSLYCYDPTNDGTGEMVAVKALKEGC
GPQLRSGWQREIEILRTLYHEHIVKYKGCCEDKSVQLVMEYVPLGSLRDY
LPRHCVGLAQLLLFAQQICEGMAYLHAQHYIHRALAARNVLLDNDRLVKI
GDFGLAKAVPEGHEYYRVREDGDSPVFWYAPECLKECKFYYASDVWSFGV
TLYELLTYCDSNQSPHTKFTELIGHTQGQMTVLRLTELLERGERLPRPDR
CPCEIYHLMKNCWETEASFRPTFQNLVPILQTAQEKYQ
3D structure
PDB4e1z Enabling structure-based drug design of Tyk2 through co-crystallization with a stabilizing aminoindazole inhibitor.
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A1019 A1021 R1023 N1024 D1037 S1059
Catalytic site (residue number reindexed from 1) A134 A136 R138 N139 D152 S174
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 0MX A R897 L899 G900 E901 G902 G905 K906 V907 A924 E975 Y976 V977 P978 G980 R1023 N1024 L1026 D1037 R15 L17 G18 E19 G20 G23 K24 V25 A42 E90 Y91 V92 P93 G95 R138 N139 L141 D152 PDBbind-CN: -logKd/Ki=8.52,IC50<3nM
Gene Ontology
Molecular Function
GO:0004672 protein 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:4e1z, PDBe:4e1z, PDBj:4e1z
PDBsum4e1z
PubMed22995073
UniProtQ9R117|TYK2_MOUSE Non-receptor tyrosine-protein kinase TYK2 (Gene Name=Tyk2)

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