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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

4RER

Crystal structure of the phosphorylated human alpha1 beta2 gamma1 holo-AMPK complex bound to AMP and cyclodextrin

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000785cellular_componentchromatin
A0001666biological_processresponse to hypoxia
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
A0004691molecular_functioncAMP-dependent protein kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005929cellular_componentcilium
A0006006biological_processglucose metabolic process
A0006325biological_processchromatin organization
A0006338biological_processchromatin remodeling
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
A0007165biological_processsignal transduction
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
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
A0033554biological_processcellular response to stress
A0034599biological_processcellular response to oxidative stress
A0036064cellular_componentciliary basal body
A0042149biological_processcellular response to glucose starvation
A0042542biological_processresponse to hydrogen peroxide
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
A0045542biological_processpositive regulation of cholesterol biosynthetic process
A0045821biological_processpositive regulation of glycolytic process
A0045893biological_processpositive regulation of DNA-templated transcription
A0046318biological_processnegative regulation of glucosylceramide biosynthetic process
A0046627biological_processnegative regulation of insulin receptor signaling pathway
A0046872molecular_functionmetal ion binding
A0047322molecular_function[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase activity
A0048156molecular_functiontau protein binding
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
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
A1904428biological_processnegative regulation of tubulin deacetylation
A1905691biological_processlipid droplet disassembly
A1990044biological_processprotein localization to lipid droplet
G0000166molecular_functionnucleotide binding
G0004679molecular_functionAMP-activated protein kinase activity
G0004691molecular_functioncAMP-dependent protein kinase activity
G0005515molecular_functionprotein binding
G0005524molecular_functionATP binding
G0005634cellular_componentnucleus
G0005654cellular_componentnucleoplasm
G0005737cellular_componentcytoplasm
G0005829cellular_componentcytosol
G0006110biological_processregulation of glycolytic process
G0006468biological_processprotein phosphorylation
G0006629biological_processlipid metabolic process
G0006631biological_processfatty acid metabolic process
G0006633biological_processfatty acid biosynthetic process
G0007165biological_processsignal transduction
G0007283biological_processspermatogenesis
G0008603molecular_functioncAMP-dependent protein kinase regulator activity
G0016020cellular_componentmembrane
G0016208molecular_functionAMP binding
G0019887molecular_functionprotein kinase regulator activity
G0019901molecular_functionprotein kinase binding
G0031588cellular_componentnucleotide-activated protein kinase complex
G0031669biological_processcellular response to nutrient levels
G0032991cellular_componentprotein-containing complex
G0042149biological_processcellular response to glucose starvation
G0043531molecular_functionADP binding
G0043609biological_processregulation of carbon utilization
G0044877molecular_functionprotein-containing complex binding
G0045722biological_processpositive regulation of gluconeogenesis
G0051170biological_processimport into nucleus
G0051726biological_processregulation of cell cycle
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGVGTFGKVKvGkheltghk..........VAVK
ChainResidueDetails
ALEU24-LYS47
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VvHrDLKpeNVLL
ChainResidueDetails
AVAL137-LEU149
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":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by LKB1 and CaMKK2","evidences":[{"source":"UniProtKB","id":"Q5EG47","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P54645","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by ULK1","evidences":[{"source":"UniProtKB","id":"P54645","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by ULK1","evidences":[{"source":"UniProtKB","id":"P54645","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18318008","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues60
DetailsDomain: {"description":"CBS 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues62
DetailsDomain: {"description":"CBS 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues62
DetailsDomain: {"description":"CBS 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues21
DetailsMotif: {"description":"AMPK pseudosubstrate"}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P80385","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17452784","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24352254","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25412657","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4CFF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by ULK1","evidences":[{"source":"UniProtKB","id":"P80385","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by ULK1","evidences":[{"source":"UniProtKB","id":"P80385","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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