Structure of PDB 6vny Chain A

Receptor sequence
>6vnyA (length=287) Species: 9606 (Homo sapiens) [Search protein sequence]
PTVFHKRYLKKIRDLGEGHFGKVSLYCYDPTNDGTGEMVAVKALKADAGP
QHRSGWKQEIDILRTLYHEHIIKYKGCCEDAGAASLQLVMEYVPLGSLRD
YLPRHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVK
IGDFGLAKAVPEGHEYYRDGDSPVFWYAPECLKEYKFYYASDVWSFGVTL
YELLTHCDSSQSPPTKFLELIGIAQGQMTVLRLTELLERGERLPRPDKCP
AEVYHLMKNCWETEASFRPTFENLIPILKTVHEKYQG
3D structure
PDB6vny Design and optimization of a series of 4-(3-azabicyclo[3.1.0]hexan-3-yl)pyrimidin-2-amines: Dual inhibitors of TYK2 and JAK1.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D1023 A1025 R1027 N1028 D1041 P1064
Catalytic site (residue number reindexed from 1) D135 A137 R139 N140 D153 P173
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 R4S A L903 G904 E905 G906 V911 A928 I960 Y980 V981 G984 S985 D988 L1030 D1041 L15 G16 E17 G18 V23 A40 I72 Y92 V93 G96 S97 D100 L142 D153 MOAD: ic50=139nM
BindingDB: IC50=1523nM
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:6vny, PDBe:6vny, PDBj:6vny
PDBsum6vny
PubMed32253095
UniProtP29597|TYK2_HUMAN Non-receptor tyrosine-protein kinase TYK2 (Gene Name=TYK2)

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