Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6B2E

Structure of full length human AMPK (a2b2g1) in complex with a small molecule activator SC4.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0002181biological_processcytoplasmic translation
A0003682molecular_functionchromatin binding
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004679molecular_functionAMP-activated protein kinase activity
A0004712molecular_functionprotein serine/threonine/tyrosine kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005794cellular_componentGolgi apparatus
A0005829cellular_componentcytosol
A0006325biological_processchromatin organization
A0006338biological_processchromatin remodeling
A0006468biological_processprotein phosphorylation
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0006646biological_processphosphatidylethanolamine biosynthetic process
A0006656biological_processphosphatidylcholine biosynthetic process
A0006694biological_processsteroid biosynthetic process
A0006695biological_processcholesterol biosynthetic process
A0006914biological_processautophagy
A0007165biological_processsignal transduction
A0008202biological_processsteroid metabolic process
A0008203biological_processcholesterol metabolic process
A0008610biological_processlipid biosynthetic process
A0009267biological_processcellular response to starvation
A0010468biological_processregulation of gene expression
A0010494cellular_componentcytoplasmic stress granule
A0010508biological_processpositive regulation of autophagy
A0010629biological_processnegative regulation of gene expression
A0014850biological_processresponse to muscle activity
A0016055biological_processWnt signaling pathway
A0016126biological_processsterol biosynthetic process
A0016239biological_processpositive regulation of macroautophagy
A0016241biological_processregulation of macroautophagy
A0016301molecular_functionkinase activity
A0016607cellular_componentnuclear speck
A0016740molecular_functiontransferase activity
A0030424cellular_componentaxon
A0030425cellular_componentdendrite
A0031588cellular_componentnucleotide-activated protein kinase complex
A0031669biological_processcellular response to nutrient levels
A0032007biological_processnegative regulation of TOR signaling
A0034198biological_processcellular response to amino acid starvation
A0034599biological_processcellular response to oxidative stress
A0036064cellular_componentciliary basal body
A0038202biological_processTORC1 signaling
A0042149biological_processcellular response to glucose starvation
A0042593biological_processglucose homeostasis
A0042752biological_processregulation of circadian rhythm
A0043025cellular_componentneuronal cell body
A0043066biological_processnegative regulation of apoptotic process
A0045821biological_processpositive regulation of glycolytic process
A0045947biological_processnegative regulation of translational initiation
A0045948biological_processpositive regulation of translational initiation
A0046872molecular_functionmetal ion binding
A0047322molecular_function[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase activity
A0048511biological_processrhythmic process
A0055089biological_processfatty acid homeostasis
A0061462biological_processprotein localization to lysosome
A0062028biological_processregulation of stress granule assembly
A0070507biological_processregulation of microtubule cytoskeleton organization
A0071277biological_processcellular response to calcium ion
A0071333biological_processcellular response to glucose stimulus
A0071380biological_processcellular response to prostaglandin E stimulus
A0071466biological_processcellular response to xenobiotic stimulus
A0085020biological_processprotein K6-linked ubiquitination
A0090200biological_processpositive regulation of release of cytochrome c from mitochondria
A0097009biological_processenergy homeostasis
A0097284biological_processhepatocyte apoptotic process
A0106310molecular_functionprotein serine kinase activity
A0140823molecular_functionhistone H2BS36 kinase activity
A1903829biological_processpositive regulation of protein localization
A1903944biological_processnegative regulation of hepatocyte apoptotic process
A1904262biological_processnegative regulation of TORC1 signaling
A1904263biological_processpositive regulation of TORC1 signaling
A1904428biological_processnegative regulation of tubulin deacetylation
A1905691biological_processlipid droplet disassembly
A1990044biological_processprotein localization to lipid droplet
B0004679molecular_functionAMP-activated protein kinase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006629biological_processlipid metabolic process
B0006631biological_processfatty acid metabolic process
B0006633biological_processfatty acid biosynthetic process
B0007165biological_processsignal transduction
B0019901molecular_functionprotein kinase binding
B0031588cellular_componentnucleotide-activated protein kinase complex
B0031669biological_processcellular response to nutrient levels
B0120162biological_processpositive regulation of cold-induced thermogenesis
C0000166molecular_functionnucleotide binding
C0004679molecular_functionAMP-activated protein kinase activity
C0004691molecular_functioncAMP-dependent protein kinase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006110biological_processregulation of glycolytic process
C0006468biological_processprotein phosphorylation
C0006629biological_processlipid metabolic process
C0006631biological_processfatty acid metabolic process
C0006633biological_processfatty acid biosynthetic process
C0007165biological_processsignal transduction
C0007283biological_processspermatogenesis
C0008603molecular_functioncAMP-dependent protein kinase regulator activity
C0016020cellular_componentmembrane
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
C0043609biological_processregulation of carbon utilization
C0044877molecular_functionprotein-containing complex binding
C0045722biological_processpositive regulation of gluconeogenesis
C0051170biological_processimport into nucleus
C0051726biological_processregulation of cell cycle
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGVGTFGKVKiGehqltghk..........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; by LKB1 and CaMKK2","evidences":[{"source":"PubMed","id":"15980064","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24767988","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28552616","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q09137","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by ULK1","evidences":[{"source":"UniProtKB","id":"Q9QZH4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
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_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues60
DetailsDomain: {"description":"CBS 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues62
DetailsDomain: {"description":"CBS 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues21
DetailsMotif: {"description":"AMPK pseudosubstrate"}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P80385","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
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_FI14
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by ULK1","evidences":[{"source":"UniProtKB","id":"P80385","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by ULK1","evidences":[{"source":"UniProtKB","id":"P80385","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

PDB statisticsPDBj update infoContact PDBjnumon