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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

5T5T

AMPK bound to allosteric activator

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004679molecular_functionAMP-activated protein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
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
C0043609biological_processregulation of carbon utilization
C0044877molecular_functionprotein-containing complex binding
C0045722biological_processpositive regulation of gluconeogenesis
C0051170biological_processimport into nucleus
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue STU A 601
ChainResidue
ALEU22
AVAL96
AGLY99
AGLU100
AGLU143
AASN144
ALEU146
AASP157
AGLY23
AVAL24
AGLY25
AVAL30
AALA43
AMET93
AGLU94
ATYR95
site_idAC2
Number of Residues2
Detailsbinding site for residue CL A 602
ChainResidue
ASER97
AALA149
site_idAC3
Number of Residues1
Detailsbinding site for residue CL A 603
ChainResidue
AGLY210
site_idAC4
Number of Residues2
Detailsbinding site for residue CL A 604
ChainResidue
AGLY23
AVAL24
site_idAC5
Number of Residues2
Detailsbinding site for residue SO4 A 605
ChainResidue
ALYS34
ALYS41
site_idAC6
Number of Residues12
Detailsbinding site for residue 75O B 4000
ChainResidue
ALEU18
AGLY19
ALYS29
ALYS31
AILE46
AASP88
BVAL81
BARG83
BASP108
BASN111
BVAL113
BILE115
site_idAC7
Number of Residues12
Detailsbinding site for residue AMP C 401
ChainResidue
CHIS150
CTHR199
CILE203
CALA204
CVAL224
CSER225
CALA226
CHIS297
CILE311
CSER313
CSER315
CASP316
site_idAC8
Number of Residues11
Detailsbinding site for residue AMP C 402
ChainResidue
CARG69
CILE239
CSER241
CPHE243
CASP244
CARG268
CLEU276
CVAL296
CHIS297
CARG298
CVAL300
site_idAC9
Number of Residues11
Detailsbinding site for residue ADP C 403
ChainResidue
CARG69
CMET84
CTHR86
CTHR88
CASP89
CTYR120
CLEU128
CVAL129
CILE149
CHIS150
CARG151
site_idAD1
Number of Residues2
Detailsbinding site for residue SO4 C 404
ChainResidue
CARG151
CTHR167
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":"Phosphothreonine; by ULK1","evidences":[{"source":"PubMed","id":"21460634","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"12764152","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
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_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q9Y478","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9R078","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues60
DetailsDomain: {"description":"CBS 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues62
DetailsDomain: {"description":"CBS 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues62
DetailsDomain: {"description":"CBS 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues21
DetailsMotif: {"description":"AMPK pseudosubstrate"}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17851531","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2V92","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues8
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_FI18
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by ULK1","evidences":[{"source":"PubMed","id":"21460634","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

243531

PDB entries from 2025-10-22

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