BioLiP

Structure of PDB 5ufu Chain A

Receptor sequence

>5ufuA (length=369) Species: 10116 (Rattus norvegicus) [Search protein sequence]

GRVKIGHYILGDTLGVGTFGKVKVGKHELTGHKVAVKILNRQKIRSLDVV
GKIRREIQNLKLFRHPHIIKLYQVISTPSDIFMVMEYVSGGELFDYICKN
GRLDEKESRRLFQQILSGVDYCHRHMVVHRDLKPENVLLDAHMNAKIADF
GLSNMMSDGEFLRTSCGSPNYAAPEVISGRLYAGPEVDIWSSGVILYALL
CGTLPFDDDHVPTLFKKICDGIFYTPQYLNPSVISLLKHMLQVDPMKRAT
IKDIREHEWFKQDLPKYLFPEAKWHLGIRSQSRPNDIMAEVCRAIKQLDY
EWKVVNPYYLRVRRKNPVTSTFSKMSLQLYQVDSRTYLLDFRSIDDERPG
SHTIEFFEMCANLIKILAQ

3D structure

PDB

5ufu Activation of Skeletal Muscle AMPK Promotes Glucose Disposal and Glucose Lowering in Non-human Primates and Mice.

Chain

Resolution

3.45 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	D139 K141 E143 N144 D157 S176
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	STU	A	L22 G23 V24 G25 V30 A43 K45 I77 E94 Y95 V96 G99 E100 E143 N144 L146 D157	L14 G15 V16 G17 V22 A35 K37 I69 E86 Y87 V88 G91 E92 E135 N136 L138 D149
BS02	85V	A	V11 L18 G19 K29 K31 I46 N48 K51 D88	V3 L10 G11 K21 K23 I38 N40 K43 D80

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

View graph for
Biological Process

PDB	RCSB:5ufu, PDBe:5ufu, PDBj:5ufu
PDBsum	5ufu
PubMed	28467931
UniProt	P54645\|AAPK1_RAT 5'-AMP-activated protein kinase catalytic subunit alpha-1 (Gene Name=Prkaa1)