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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

5EZV

X-ray crystal structure of AMP-activated protein kinase alpha-2/alpha-1 RIM chimaera (alpha-2(1-347)/alpha-1(349-401)/alpha-2(397-end) beta-1 gamma-1) co-crystallized with C2 (5-(5-hydroxyl-isoxazol-3-yl)-furan-2-phosphonic acid)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004679molecular_functionAMP-activated protein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005788cellular_componentendoplasmic reticulum lumen
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
B0032991cellular_componentprotein-containing complex
B0120162biological_processpositive regulation of cold-induced thermogenesis
C0004672molecular_functionprotein kinase activity
C0004679molecular_functionAMP-activated protein kinase activity
C0005524molecular_functionATP binding
C0006468biological_processprotein phosphorylation
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005788cellular_componentendoplasmic reticulum lumen
D0005829cellular_componentcytosol
D0006629biological_processlipid metabolic process
D0006631biological_processfatty acid metabolic process
D0006633biological_processfatty acid biosynthetic process
D0007165biological_processsignal transduction
D0019901molecular_functionprotein kinase binding
D0031588cellular_componentnucleotide-activated protein kinase complex
D0031669biological_processcellular response to nutrient levels
D0032991cellular_componentprotein-containing complex
D0120162biological_processpositive regulation of cold-induced thermogenesis
E0000166molecular_functionnucleotide binding
E0004679molecular_functionAMP-activated protein kinase activity
E0004691molecular_functioncAMP-dependent protein kinase activity
E0005515molecular_functionprotein binding
E0005524molecular_functionATP binding
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005737cellular_componentcytoplasm
E0005788cellular_componentendoplasmic reticulum lumen
E0005829cellular_componentcytosol
E0006110biological_processregulation of glycolytic process
E0006468biological_processprotein phosphorylation
E0006629biological_processlipid metabolic process
E0006631biological_processfatty acid metabolic process
E0006633biological_processfatty acid biosynthetic process
E0007165biological_processsignal transduction
E0007283biological_processspermatogenesis
E0008603molecular_functioncAMP-dependent protein kinase regulator activity
E0016020cellular_componentmembrane
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
E0044877molecular_functionprotein-containing complex binding
E0045722biological_processpositive regulation of gluconeogenesis
E0051726biological_processregulation of cell cycle
F0000166molecular_functionnucleotide binding
F0004679molecular_functionAMP-activated protein kinase activity
F0004691molecular_functioncAMP-dependent protein kinase activity
F0005515molecular_functionprotein binding
F0005524molecular_functionATP binding
F0005634cellular_componentnucleus
F0005654cellular_componentnucleoplasm
F0005737cellular_componentcytoplasm
F0005788cellular_componentendoplasmic reticulum lumen
F0005829cellular_componentcytosol
F0006110biological_processregulation of glycolytic process
F0006468biological_processprotein phosphorylation
F0006629biological_processlipid metabolic process
F0006631biological_processfatty acid metabolic process
F0006633biological_processfatty acid biosynthetic process
F0007165biological_processsignal transduction
F0007283biological_processspermatogenesis
F0008603molecular_functioncAMP-dependent protein kinase regulator activity
F0016020cellular_componentmembrane
F0016208molecular_functionAMP binding
F0019887molecular_functionprotein kinase regulator activity
F0019901molecular_functionprotein kinase binding
F0031588cellular_componentnucleotide-activated protein kinase complex
F0031669biological_processcellular response to nutrient levels
F0032991cellular_componentprotein-containing complex
F0042149biological_processcellular response to glucose starvation
F0043531molecular_functionADP binding
F0044877molecular_functionprotein-containing complex binding
F0045722biological_processpositive regulation of gluconeogenesis
F0051726biological_processregulation of cell cycle
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue STU A 601
ChainResidue
ALEU22
AVAL96
AGLU100
AGLU143
AASN144
ALEU146
AGLY23
AVAL24
AGLY25
AVAL30
AALA43
AMET93
AGLU94
ATYR95
site_idAC2
Number of Residues10
Detailsbinding site for residue C1V A 602
ChainResidue
ALEU18
AGLY19
ALYS29
ALYS31
AILE46
AASP88
BARG83
BTHR106
BSEP108
BVAL113
site_idAC3
Number of Residues14
Detailsbinding site for residue STU C 601
ChainResidue
CLEU22
CGLY23
CVAL24
CGLY25
CVAL30
CALA43
CGLU94
CTYR95
CVAL96
CGLU100
CGLU143
CASN144
CLEU146
CASP157
site_idAC4
Number of Residues12
Detailsbinding site for residue C1V C 602
ChainResidue
CVAL11
CLEU18
CGLY19
CLYS29
CLYS31
CILE46
CASN48
CASP88
DARG83
DARG107
DSEP108
DVAL113
site_idAC5
Number of Residues8
Detailsbinding site for residue C2Z E 401
ChainResidue
EHIS151
EARG152
ESER226
EHIS298
EARG299
ESER314
ESER316
EC2Z402
site_idAC6
Number of Residues10
Detailsbinding site for residue C2Z E 402
ChainResidue
EARG70
ETHR87
ETHR89
EHIS151
ESER226
ESER242
ELYS243
EPHE244
EARG299
EC2Z401
site_idAC7
Number of Residues8
Detailsbinding site for residue C2Z F 401
ChainResidue
FHIS151
FARG152
FSER226
FHIS298
FARG299
FSER314
FSER316
FC2Z402
site_idAC8
Number of Residues11
Detailsbinding site for residue C2Z F 402
ChainResidue
FARG70
FTHR87
FTHR89
FHIS151
FSER226
FSER242
FLYS243
FPHE244
FHIS298
FARG299
FC2Z401
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 Residues2
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 Residues18
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by LKB1 and CaMKK2","evidences":[{"source":"UniProtKB","id":"Q5EG47","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P54645","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by ULK1","evidences":[{"source":"UniProtKB","id":"P54645","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P80386","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18088087","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":"20068231","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_FI11
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9R078","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues120
DetailsDomain: {"description":"CBS 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues124
DetailsDomain: {"description":"CBS 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues124
DetailsDomain: {"description":"CBS 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues42
DetailsMotif: {"description":"AMPK pseudosubstrate"}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues32
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P80385","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues16
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_FI19
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine; by ULK1","evidences":[{"source":"UniProtKB","id":"P80385","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by ULK1","evidences":[{"source":"UniProtKB","id":"P80385","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

248335

PDB entries from 2026-01-28

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