Structure of PDB 6c9h Chain A

Receptor sequence
>6c9hA (length=435) Species: 9606 (Homo sapiens) [Search protein sequence]
GSVKIGHYILGDTLGVGTFGKVKVGKHELTGHKVAVKILNRQKIRSLDVV
GKIRREIQNLKLFRHPHIIKLYQVISTPSDIFMVMEYVSGGELFDYICKN
GRLDEKESRRLFQQILSGVDYCHRHMVVHRDLKPENVLLDAHMNAKIADF
GLSNMMSDGEFLRTSCGSPNYAAPEVISGRLYAGPEVDIWSSGVILYALL
CGTLPFDDDHVPTLFKKICDGIFYTPQYLNPSVISLLKHMLQVDPMKRAT
IKDIREHEWFKQDLPKYLFPEDPSYSSTMIDDEALKEVLYNRNHQDPLAV
AYHLIIDNRRIMNEAKDFYLATSPTRPHPERVPFKAKWHLGIRSQSRPND
IMAEVCRAIKQLDYEWKVVNPYYLRVRRKNPVTSTYSKMSLQLYQVDSRT
YLLDFRSIDDELTPRPGSHTIEFFEMCANLIKILA
3D structure
PDB6c9h Structures of AMP-activated protein kinase bound to novel pharmacological activators in phosphorylated, non-phosphorylated, and nucleotide-free states.
ChainA
Resolution2.65 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D141 K143 E145 N146 D159 S178
Catalytic site (residue number reindexed from 1) D131 K133 E135 N136 D149 S168
Enzyme Commision number 2.7.11.1: non-specific serine/threonine protein kinase.
2.7.11.26: [tau protein] kinase.
2.7.11.31: [hydroxymethylglutaryl-CoA reductase (NADPH)] 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 R34 A V13 L20 F29 K33 I48 N50 D90 V3 L10 F19 K23 I38 N40 D80
BS02 STU A G25 A45 K47 M95 Y97 V98 G101 E102 E145 N146 L148 D159 G15 A35 K37 M85 Y87 V88 G91 E92 E135 N136 L138 D149
Gene Ontology
Molecular Function
GO:0004672 protein kinase activity
GO:0004679 AMP-activated 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:6c9h, PDBe:6c9h, PDBj:6c9h
PDBsum6c9h
PubMed30478170
UniProtQ13131|AAPK1_HUMAN 5'-AMP-activated protein kinase catalytic subunit alpha-1 (Gene Name=PRKAA1)

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