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4EAK

Co-crystal structure of an AMPK core with ATP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004679molecular_functionAMP-activated protein kinase activity
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 Residues17
DetailsBINDING SITE FOR RESIDUE ATP C 401
ChainResidue
CARG69
CILE149
CHIS150
CARG151
CPRO153
CPHE243
CHOH501
CHOH506
CHOH520
CMET84
CTHR86
CILE87
CTHR88
CASP89
CGLN122
CPRO127
CVAL129

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE ATP C 402
ChainResidue
CHIS150
CTHR199
CILE203
CALA204
CVAL224
CSER225
CALA226
CHIS297
CARG298
CILE311
CSER313
CLEU314
CSER315
CASP316
CHOH502

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE TAM C 403
ChainResidue
CARG69
CLYS169
CARG170
CHIS297

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q13131","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues62
DetailsDomain: {"description":"CBS 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues21
DetailsMotif: {"description":"AMPK pseudosubstrate"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17851531","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2V92","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
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_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by ULK1","evidences":[{"source":"PubMed","id":"21460634","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by ULK1","evidences":[{"source":"PubMed","id":"21460634","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by ULK1","evidences":[{"source":"PubMed","id":"21460634","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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