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2Y8Q

Structure of the regulatory fragment of mammalian AMPK in complex with one ADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0004679molecular_functionAMP-activated protein kinase activity
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 Residues11
DetailsBINDING SITE FOR RESIDUE ADP E 1327
ChainResidue
EMET84
EARG151
EPRO153
ETHR86
ETHR88
EASP89
EPRO127
ELEU128
EVAL129
EILE149
EHIS150

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE AMP E 1328
ChainResidue
AARG457
EHIS150
ETHR199
EILE203
EALA204
EVAL224
ESER225
EALA226
EPRO228
EILE311
ESER313
ESER315
EASP316
EHOH2039

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

site_idSWS_FT_FI3
Number of Residues62
DetailsDomain: {"description":"CBS 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues62
DetailsDomain: {"description":"CBS 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues21
DetailsMotif: {"description":"AMPK pseudosubstrate"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17851531","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2V92","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
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_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by ULK1","evidences":[{"source":"PubMed","id":"21460634","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by ULK1","evidences":[{"source":"PubMed","id":"21460634","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by ULK1","evidences":[{"source":"PubMed","id":"21460634","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

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