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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

4QFS

Structure of AMPK in complex with Br2-A769662core activator and STAUROSPORINE inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000785cellular_componentchromatin
A0002842biological_processpositive regulation of T cell mediated immune response to tumor cell
A0003682molecular_functionchromatin binding
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004679molecular_functionAMP-activated protein kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006006biological_processglucose metabolic process
A0006325biological_processchromatin organization
A0006338biological_processchromatin remodeling
A0006351biological_processDNA-templated transcription
A0006468biological_processprotein phosphorylation
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0006694biological_processsteroid biosynthetic process
A0006695biological_processcholesterol biosynthetic process
A0006914biological_processautophagy
A0008202biological_processsteroid metabolic process
A0008203biological_processcholesterol metabolic process
A0008284biological_processpositive regulation of cell population proliferation
A0008610biological_processlipid biosynthetic process
A0009267biological_processcellular response to starvation
A0009410biological_processresponse to xenobiotic stimulus
A0009411biological_processresponse to UV
A0009631biological_processcold acclimation
A0010332biological_processresponse to gamma radiation
A0010508biological_processpositive regulation of autophagy
A0010628biological_processpositive regulation of gene expression
A0010629biological_processnegative regulation of gene expression
A0014823biological_processresponse to activity
A0016055biological_processWnt signaling pathway
A0016126biological_processsterol biosynthetic process
A0016301molecular_functionkinase activity
A0016324cellular_componentapical plasma membrane
A0016607cellular_componentnuclear speck
A0016740molecular_functiontransferase activity
A0017148biological_processnegative regulation of translation
A0019395biological_processfatty acid oxidation
A0030424cellular_componentaxon
A0030425cellular_componentdendrite
A0031000biological_processresponse to caffeine
A0031588cellular_componentnucleotide-activated protein kinase complex
A0031669biological_processcellular response to nutrient levels
A0032007biological_processnegative regulation of TOR signaling
A0032991cellular_componentprotein-containing complex
A0033135biological_processregulation of peptidyl-serine phosphorylation
A0033554biological_processcellular response to stress
A0034599biological_processcellular response to oxidative stress
A0042149biological_processcellular response to glucose starvation
A0042542biological_processresponse to hydrogen peroxide
A0042557molecular_functioneukaryotic elongation factor-2 kinase activator activity
A0042593biological_processglucose homeostasis
A0042752biological_processregulation of circadian rhythm
A0043025cellular_componentneuronal cell body
A0043066biological_processnegative regulation of apoptotic process
A0043114biological_processregulation of vascular permeability
A0043627biological_processresponse to estrogen
A0044877molecular_functionprotein-containing complex binding
A0045722biological_processpositive regulation of gluconeogenesis
A0045821biological_processpositive regulation of glycolytic process
A0045893biological_processpositive regulation of DNA-templated transcription
A0046321biological_processpositive regulation of fatty acid oxidation
A0046326biological_processpositive regulation of D-glucose import
A0046627biological_processnegative regulation of insulin receptor signaling pathway
A0046872molecular_functionmetal ion binding
A0047322molecular_function[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase activity
A0048511biological_processrhythmic process
A0048643biological_processpositive regulation of skeletal muscle tissue development
A0050321molecular_functiontau-protein kinase activity
A0050870biological_processpositive regulation of T cell activation
A0050995biological_processnegative regulation of lipid catabolic process
A0055089biological_processfatty acid homeostasis
A0060627biological_processregulation of vesicle-mediated transport
A0061744biological_processmotor behavior
A0061762biological_processCAMKK-AMPK signaling cascade
A0062028biological_processregulation of stress granule assembly
A0070050biological_processneuron cellular homeostasis
A0070301biological_processcellular response to hydrogen peroxide
A0070507biological_processregulation of microtubule cytoskeleton organization
A0071277biological_processcellular response to calcium ion
A0071333biological_processcellular response to glucose stimulus
A0071361biological_processcellular response to ethanol
A0071380biological_processcellular response to prostaglandin E stimulus
A0071456biological_processcellular response to hypoxia
A0071466biological_processcellular response to xenobiotic stimulus
A0072657biological_processprotein localization to membrane
A0072659biological_processprotein localization to plasma membrane
A0097009biological_processenergy homeostasis
A0106310molecular_functionprotein serine kinase activity
A0110076biological_processnegative regulation of ferroptosis
A0140823molecular_functionhistone H2BS36 kinase activity
A1903109biological_processpositive regulation of mitochondrial transcription
A1903829biological_processpositive regulation of protein localization
A1903944biological_processnegative regulation of hepatocyte apoptotic process
A1903955biological_processpositive regulation of protein targeting to mitochondrion
A1904179biological_processpositive regulation of adipose tissue development
A1904262biological_processnegative regulation of TORC1 signaling
A1905691biological_processlipid droplet disassembly
A1990044biological_processprotein localization to lipid droplet
C0000166molecular_functionnucleotide binding
C0004679molecular_functionAMP-activated protein kinase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006110biological_processregulation of glycolytic process
C0006629biological_processlipid metabolic process
C0006631biological_processfatty acid metabolic process
C0006633biological_processfatty acid biosynthetic process
C0016208molecular_functionAMP binding
C0019887molecular_functionprotein kinase regulator activity
C0019901molecular_functionprotein kinase binding
C0031588cellular_componentnucleotide-activated protein kinase complex
C0031669biological_processcellular response to nutrient levels
C0032991cellular_componentprotein-containing complex
C0042149biological_processcellular response to glucose starvation
C0043531molecular_functionADP binding
C0044877molecular_functionprotein-containing complex binding
C0045722biological_processpositive regulation of gluconeogenesis
C0050790biological_processregulation of catalytic activity
C0051170biological_processimport into nucleus
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE STU A 601
ChainResidue
ALEU22
AGLU100
AGLU143
AASN144
ALEU146
AALA156
AASP157
AGLY23
AGLY25
AVAL30
AALA43
AILE77
AGLU94
ATYR95
AVAL96
site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE 32H A 602
ChainResidue
ALYS29
AILE46
ALYS51
AASP88
BARG83
BASP108
BVAL113
site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 603
ChainResidue
AVAL24
site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 606
ChainResidue
ASER97
AALA149
site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL B 301
ChainResidue
BTHR85
BASP136
site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE AMP C 401
ChainResidue
CHIS150
CILE203
CALA204
CVAL224
CSER225
CALA226
CHIS297
CSER313
CSER315
CASP316
site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 402
ChainResidue
CARG69
CTHR86
CTHR88
CILE149
CHIS150
CARG151
site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 C 403
ChainResidue
CARG69
CSER241
CPHE243
CHIS297
CARG298
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGVGTFGKVKvGkheltghk..........VAVK
ChainResidueDetails
ALEU22-LYS45
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VvHrDLKpeNVLL
ChainResidueDetails
AVAL135-LEU147
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q13131","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by LKB1 and CaMKK2","evidences":[{"source":"PubMed","id":"14511394","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14614828","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16054095","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16054096","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8910387","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"12764152","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q13131","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"12764152","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"11171104","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12764152","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9305909","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22673903","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q9Y478","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9R078","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues60
DetailsDomain: {"description":"CBS 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues21
DetailsMotif: {"description":"AMPK pseudosubstrate"}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17851531","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2V92","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17851531","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21399626","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2V8Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2Y8L","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by ULK1","evidences":[{"source":"PubMed","id":"21460634","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by ULK1","evidences":[{"source":"PubMed","id":"21460634","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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