Structure of PDB 6ao5 Chain A

Receptor sequence
>6ao5A (length=321) Species: 9606 (Homo sapiens) [Search protein sequence]
DVLEKLGEGSYGSVFKAIHVVAIKQDLQEIIKEISIMQQCDSPYVVKYYG
SYFLWIVMEYCGAGSVSDIIRLRNKTLIEDEIATILKSTLKGLEYLHFMR
KIHRNIKAGNILLNTEGHAKLADFGVAVIGTPFWMAPEVIQEIGYNCVAD
IWSLGITSIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDDFTD
FVKKCLVKNPEQRATATQLLQHPFIKNAKPVSILRDLITEAMEIKAKRHE
EQQRELEEEENWKVPQDGDFDFLKNLSLEELQMRLKALDPMMEREIEELR
QRYTAKRQPILDAMDAKKRRQ
3D structure
PDB6ao5 SAV1 promotes Hippo kinase activation through antagonizing the PP2A phosphatase STRIPAK.
ChainA
Resolution2.955 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N146 K148 G150 N151 D164 T184
Catalytic site (residue number reindexed from 1) N105 K107 G109 N110 D123 T131
Enzyme Commision number 2.7.11.1: non-specific serine/threonine protein 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 ANP A E35 S37 Y38 V41 A54 K56 M99 C102 D109 N151 L153 D164 E8 S10 Y11 V14 A22 K24 M58 C61 D68 N110 L112 D123
BS02 MG A N151 D164 N110 D123
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004674 protein serine/threonine kinase activity
GO:0005524 ATP binding
Biological Process
GO:0006468 protein phosphorylation
GO:0007165 signal transduction

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Molecular Function
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Biological Process
External links
PDB RCSB:6ao5, PDBe:6ao5, PDBj:6ao5
PDBsum6ao5
PubMed29063833
UniProtQ13188|STK3_HUMAN Serine/threonine-protein kinase 3 (Gene Name=STK3)

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