Structure of PDB 6c9j Chain A

Receptor sequence
>6c9jA (length=386) Species: 9606 (Homo sapiens) [Search protein sequence]
GSVKIGHYILGDTLGVGTFGKVKVGKHELTGHKVAVKILNRQKIRSLDVV
GKIRREIQNLKLFRHPHIIKLYQVISTPSDIFMVMEYVSGGELFDYICKN
GRLDEKESRRLFQQILSGVDYCHRHMVVHRDLKPENVLLDAHMNAKIADF
GLSNMMSDGEFLRTSCGSPNYAAPEVISGRLYAGPEVDIWSSGVILYALL
CGTLPFDDDHVPTLFKKICDGIFYTPQYLNPSVISLLKHMLQVDPMKRAT
IKDIREHEWFKQDLPKYLFPETRPHPERVPFLVAKAKWHLGIRSQSRPND
IMAEVCRAIKQLDYEWKVVNPYYLRVRRKNPVTSTYSKMSLQLYQVDSRT
YLLDFRSIDDELTPRPGSHTIEFFEMCANLIKILAQ
3D structure
PDB6c9j Structures of AMP-activated protein kinase bound to novel pharmacological activators in phosphorylated, non-phosphorylated, and nucleotide-free states.
ChainA
Resolution3.05 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 K33 K53 D90 V3 L10 K23 K43 D80
BS02 STU A G25 V26 G27 A45 M95 E96 Y97 V98 G101 E102 E145 N146 L148 D159 G15 V16 G17 A35 M85 E86 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

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:6c9j, PDBe:6c9j, PDBj:6c9j
PDBsum6c9j
PubMed30478170
UniProtQ13131|AAPK1_HUMAN 5'-AMP-activated protein kinase catalytic subunit alpha-1 (Gene Name=PRKAA1)

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