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4CFH

Structure of an active form of mammalian AMPK

Replaces:  2Y94
Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
E0000166molecular_functionnucleotide binding
E0004679molecular_functionAMP-activated protein kinase activity
E0005515molecular_functionprotein binding
E0005524molecular_functionATP binding
E0005634cellular_componentnucleus
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0006110biological_processregulation of glycolytic process
E0006629biological_processlipid metabolic process
E0006631biological_processfatty acid metabolic process
E0006633biological_processfatty acid biosynthetic process
E0016208molecular_functionAMP binding
E0019887molecular_functionprotein kinase regulator activity
E0019901molecular_functionprotein kinase binding
E0031588cellular_componentnucleotide-activated protein kinase complex
E0031669biological_processcellular response to nutrient levels
E0032991cellular_componentprotein-containing complex
E0042149biological_processcellular response to glucose starvation
E0043531molecular_functionADP binding
E0043609biological_processregulation of carbon utilization
E0044877molecular_functionprotein-containing complex binding
E0045722biological_processpositive regulation of gluconeogenesis
E0051170biological_processimport into nucleus
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE AMP E 1325
ChainResidue
EARG69
EVAL296
EHIS297
EARG298
ELYS169
EILE239
ESER241
EPHE243
EASP244
EARG268
EVAL275
ELEU276

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE AMP E 1326
ChainResidue
EHIS150
ETHR199
EILE203
EALA204
EVAL224
ESER225
EALA226
EHIS297
EILE311
ESER313
ESER315
EASP316

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE STU A 1550
ChainResidue
ALEU22
AGLY23
AVAL24
AGLY25
AALA43
ALYS45
AMET93
AGLU94
ATYR95
AVAL96
AGLY99
AGLU100
AGLU143
AASN144
ALEU146
AASP157

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 Residues2
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 Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q13131","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by ULK1","evidences":[{"source":"PubMed","id":"21460634","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by ULK1","evidences":[{"source":"PubMed","id":"21460634","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by ULK1","evidences":[{"source":"PubMed","id":"21460634","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues60
DetailsDomain: {"description":"CBS 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues62
DetailsDomain: {"description":"CBS 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues62
DetailsDomain: {"description":"CBS 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues21
DetailsMotif: {"description":"AMPK pseudosubstrate"}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17851531","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2V92","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI15
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

243083

PDB entries from 2025-10-15

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