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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
B0005829cellular_componentcytosol
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
B0035878biological_processnail development
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
D0005829cellular_componentcytosol
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
D0035878biological_processnail development
D0120162biological_processpositive regulation of cold-induced thermogenesis
E0004691molecular_functioncAMP-dependent protein kinase activity
E0005515molecular_functionprotein binding
E0005524molecular_functionATP binding
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0006110biological_processregulation of glycolytic process
E0006468biological_processprotein phosphorylation
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
E0042149biological_processcellular response to glucose starvation
E0043531molecular_functionADP binding
E0043609biological_processregulation of carbon utilization
E0045722biological_processpositive regulation of gluconeogenesis
E0045860biological_processpositive regulation of protein kinase activity
E0051170biological_processimport into nucleus
F0004691molecular_functioncAMP-dependent protein kinase activity
F0005515molecular_functionprotein binding
F0005524molecular_functionATP binding
F0005634cellular_componentnucleus
F0005654cellular_componentnucleoplasm
F0005737cellular_componentcytoplasm
F0005829cellular_componentcytosol
F0006110biological_processregulation of glycolytic process
F0006468biological_processprotein phosphorylation
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
F0042149biological_processcellular response to glucose starvation
F0043531molecular_functionADP binding
F0043609biological_processregulation of carbon utilization
F0045722biological_processpositive regulation of gluconeogenesis
F0045860biological_processpositive regulation of protein kinase activity
F0051170biological_processimport into nucleus
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 Residues16
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P80385
ChainResidueDetails
EARG70
FMET85
FVAL130
FARG152
FLYS170
FSER242
FARG269
FLEU277
EMET85
EVAL130
EARG152
ELYS170
ESER242
EARG269
ELEU277
FARG70

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:17452784, ECO:0000269|PubMed:24352254, ECO:0000269|PubMed:25412657, ECO:0007744|PDB:4CFF
ChainResidueDetails
EHIS151
FSER226
FHIS298
FSER314
ETHR200
EALA205
ESER226
EHIS298
ESER314
FHIS151
FTHR200
FALA205

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphoserine; by ULK1 => ECO:0000250|UniProtKB:P80385
ChainResidueDetails
ESER261
ESER270
FSER261
FSER270

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by ULK1 => ECO:0000250|UniProtKB:P80385
ChainResidueDetails
ETHR263
FTHR263
DSER24
DSER25

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER40
DSER40

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
BSER96
DSER96

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P80386
ChainResidueDetails
BSER101
DSER101

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
BSEP108
DSEP108

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19369195
ChainResidueDetails
BTHR148
DTHR148

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9R078
ChainResidueDetails
BSER182
DSER182

site_idSWS_FT_FI11
Number of Residues2
DetailsLIPID: N-myristoyl glycine => ECO:0000269|PubMed:21680840
ChainResidueDetails
BGLY2
DGLY2

227344

PDB entries from 2024-11-13

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