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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

3G2G

S437Y Mutant of human muscle pyruvate kinase, isoform M2

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0003723molecular_functionRNA binding
A0003729molecular_functionmRNA binding
A0003824molecular_functioncatalytic activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0004715molecular_functionnon-membrane spanning protein tyrosine kinase activity
A0004743molecular_functionpyruvate kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005791cellular_componentrough endoplasmic reticulum
A0005829cellular_componentcytosol
A0005929cellular_componentcilium
A0006096biological_processglycolytic process
A0006417biological_processregulation of translation
A0012501biological_processprogrammed cell death
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0023026molecular_functionMHC class II protein complex binding
A0030955molecular_functionpotassium ion binding
A0031982cellular_componentvesicle
A0032869biological_processcellular response to insulin stimulus
A0034774cellular_componentsecretory granule lumen
A0045296molecular_functioncadherin binding
A0046872molecular_functionmetal ion binding
A0061621biological_processcanonical glycolysis
A0070062cellular_componentextracellular exosome
A1903561cellular_componentextracellular vesicle
A1903672biological_processpositive regulation of sprouting angiogenesis
A1904813cellular_componentficolin-1-rich granule lumen
A2000767biological_processpositive regulation of cytoplasmic translation
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0003723molecular_functionRNA binding
B0003729molecular_functionmRNA binding
B0003824molecular_functioncatalytic activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0004715molecular_functionnon-membrane spanning protein tyrosine kinase activity
B0004743molecular_functionpyruvate kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005791cellular_componentrough endoplasmic reticulum
B0005829cellular_componentcytosol
B0005929cellular_componentcilium
B0006096biological_processglycolytic process
B0006417biological_processregulation of translation
B0012501biological_processprogrammed cell death
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0023026molecular_functionMHC class II protein complex binding
B0030955molecular_functionpotassium ion binding
B0031982cellular_componentvesicle
B0032869biological_processcellular response to insulin stimulus
B0034774cellular_componentsecretory granule lumen
B0045296molecular_functioncadherin binding
B0046872molecular_functionmetal ion binding
B0061621biological_processcanonical glycolysis
B0070062cellular_componentextracellular exosome
B1903561cellular_componentextracellular vesicle
B1903672biological_processpositive regulation of sprouting angiogenesis
B1904813cellular_componentficolin-1-rich granule lumen
B2000767biological_processpositive regulation of cytoplasmic translation
C0000166molecular_functionnucleotide binding
C0000287molecular_functionmagnesium ion binding
C0003723molecular_functionRNA binding
C0003729molecular_functionmRNA binding
C0003824molecular_functioncatalytic activity
C0004674molecular_functionprotein serine/threonine kinase activity
C0004713molecular_functionprotein tyrosine kinase activity
C0004715molecular_functionnon-membrane spanning protein tyrosine kinase activity
C0004743molecular_functionpyruvate kinase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005576cellular_componentextracellular region
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005739cellular_componentmitochondrion
C0005791cellular_componentrough endoplasmic reticulum
C0005829cellular_componentcytosol
C0005929cellular_componentcilium
C0006096biological_processglycolytic process
C0006417biological_processregulation of translation
C0012501biological_processprogrammed cell death
C0016301molecular_functionkinase activity
C0016740molecular_functiontransferase activity
C0023026molecular_functionMHC class II protein complex binding
C0030955molecular_functionpotassium ion binding
C0031982cellular_componentvesicle
C0032869biological_processcellular response to insulin stimulus
C0034774cellular_componentsecretory granule lumen
C0045296molecular_functioncadherin binding
C0046872molecular_functionmetal ion binding
C0061621biological_processcanonical glycolysis
C0070062cellular_componentextracellular exosome
C1903561cellular_componentextracellular vesicle
C1903672biological_processpositive regulation of sprouting angiogenesis
C1904813cellular_componentficolin-1-rich granule lumen
C2000767biological_processpositive regulation of cytoplasmic translation
D0000166molecular_functionnucleotide binding
D0000287molecular_functionmagnesium ion binding
D0003723molecular_functionRNA binding
D0003729molecular_functionmRNA binding
D0003824molecular_functioncatalytic activity
D0004674molecular_functionprotein serine/threonine kinase activity
D0004713molecular_functionprotein tyrosine kinase activity
D0004715molecular_functionnon-membrane spanning protein tyrosine kinase activity
D0004743molecular_functionpyruvate kinase activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005576cellular_componentextracellular region
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005739cellular_componentmitochondrion
D0005791cellular_componentrough endoplasmic reticulum
D0005829cellular_componentcytosol
D0005929cellular_componentcilium
D0006096biological_processglycolytic process
D0006417biological_processregulation of translation
D0012501biological_processprogrammed cell death
D0016301molecular_functionkinase activity
D0016740molecular_functiontransferase activity
D0023026molecular_functionMHC class II protein complex binding
D0030955molecular_functionpotassium ion binding
D0031982cellular_componentvesicle
D0032869biological_processcellular response to insulin stimulus
D0034774cellular_componentsecretory granule lumen
D0045296molecular_functioncadherin binding
D0046872molecular_functionmetal ion binding
D0061621biological_processcanonical glycolysis
D0070062cellular_componentextracellular exosome
D1903561cellular_componentextracellular vesicle
D1903672biological_processpositive regulation of sprouting angiogenesis
D1904813cellular_componentficolin-1-rich granule lumen
D2000767biological_processpositive regulation of cytoplasmic translation
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 532
ChainResidue
ATHR432
ALYS433
ASER434
AARG436
ATYR437
site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 533
ChainResidue
AHIS274
AGLU275
AARG278
site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE UNX A 535
ChainResidue
ALYS433
AARG455
ATHR432
site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE UNX A 536
ChainResidue
AARG342
ASER346
BVAL306
BHOH566
BHOH600
site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE UNX A 537
ChainResidue
AASN75
ASER77
AASP113
ATHR114
AHOH588
site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 532
ChainResidue
BTHR432
BLYS433
BSER434
BARG436
BTYR437
site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 533
ChainResidue
BSER77
BHIS78
BGLY79
site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 534
ChainResidue
BHIS274
BGLU275
BARG278
BHOH619
DHOH580
site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE UNX B 535
ChainResidue
BASN75
BSER77
BASP113
BTHR114
BLYS270
BHOH652
site_idBC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE UNX B 536
ChainResidue
BARG73
site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE UNX B 537
ChainResidue
BHIS78
BARG120
site_idBC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE UNX B 538
ChainResidue
BGLU260
BLYS261
site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE UNX B 539
ChainResidue
BALA293
BARG294
BGLY295
BTHR328
site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE UNX B 540
ChainResidue
BGLY46
BASN70
BHIS464
BHOH549
site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE UNX B 541
ChainResidue
BCYS317
BASN318
BLYS322
BASP357
BARG445
BHOH560
site_idBC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE UNX B 542
ChainResidue
ATHR341
AALA343
BGLN329
BGLU332
BGLU344
site_idBC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE UNX B 543
ChainResidue
AASN350
BGLN310
BLYS311
BASN350
BASP354
BHOH561
site_idBC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE UNX B 544
ChainResidue
BMET334
BILE335
BGLU364
BGLY368
BASP369
BTYR370
BPRO371
site_idCC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE UNX B 545
ChainResidue
BVAL251
BHIS252
BARG255
BALA286
site_idCC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE UNX B 546
ChainResidue
BARG279
BASP281
BGLU282
BHOH563
BHOH672
site_idCC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 C 532
ChainResidue
CTHR432
CLYS433
CSER434
CARG436
CTYR437
site_idCC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 C 533
ChainResidue
CHIS78
CGLY79
CLYS206
site_idCC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 C 534
ChainResidue
CHIS78
CARG120
CHOH603
CHOH633
CHOH652
site_idCC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 C 535
ChainResidue
CHIS274
CGLU275
CARG278
site_idCC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE UNX C 536
ChainResidue
CARG73
site_idCC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE UNX C 537
ChainResidue
CTHR432
CARG455
CHOH579
site_idCC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE UNX C 538
ChainResidue
CLEU380
CARG383
CGLU384
CHOH595
site_idDC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE UNX C 539
ChainResidue
CASN75
CSER77
CASP113
CTHR114
CHOH566
site_idDC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE UNX C 540
ChainResidue
CTHR95
CTYR105
CPRO107
CVAL108
CARG461
CHOH625
site_idDC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE UNX C 541
ChainResidue
CGLN17
CALA20
CARG32
CHOH630
site_idDC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE UNX C 542
ChainResidue
CTHR328
CMET360
CLEU361
CSER362
CHOH565
site_idDC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 D 532
ChainResidue
DTHR432
DLYS433
DSER434
DARG436
DTYR437
DPHE521
DHOH623
site_idDC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 D 533
ChainResidue
DHIS78
DGLY79
site_idDC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SO4 D 534
ChainResidue
DARG436
DHIS439
site_idDC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 D 535
ChainResidue
DHIS274
DGLU275
DARG278
site_idDC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE UNX D 536
ChainResidue
DGLU272
DASP296
DUNX537
site_idEC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE UNX D 537
ChainResidue
DUNX536
DUNX538
site_idEC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE UNX D 538
ChainResidue
DASN75
DSER77
DASP113
DTHR114
DSER243
DLYS270
DUNX537
site_idEC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE UNX D 539
ChainResidue
DGLU260
DLYS261
site_idEC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE UNX D 540
ChainResidue
DLEU394
DGLU397
site_idEC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE UNX D 541
ChainResidue
DARG92
DASP236
DASP238
DARG461
site_idEC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE UNX D 542
ChainResidue
DPRO53
DARG56
DSER57
site_idEC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE UNX D 543
ChainResidue
DTHR432
DARG455
DHOH544
DHOH545
Functional Information from PROSITE/UniProt
site_idPS00110
Number of Residues13
DetailsPYRUVATE_KINASE Pyruvate kinase active site signature. IkIISKIENhEGV
ChainResidueDetails
AILE265-VAL277
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"23064226","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P30613","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues40
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"23530218","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4FXF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues33
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15996096","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23530218","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1T5A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FXF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P00549","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
DetailsSite: {"description":"Crucial for phosphotyrosine binding","evidences":[{"source":"PubMed","id":"27199445","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"16964243","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"17081983","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18088087","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18691976","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_FI8
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues8
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues8
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues8
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P11980","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues8
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"21700219","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues8
DetailsModified residue: {"description":"4-hydroxyproline","evidences":[{"source":"PubMed","id":"21620138","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues8
DetailsModified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"30487609","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"24120661","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26787900","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues12
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues132
DetailsRegion: {"description":"Intersubunit contact"}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues3
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues3
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues224
DetailsRegion: {"description":"Interaction with POU5F1","evidences":[{"source":"PubMed","id":"18191611","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
ATHR328
ASER362
AGLU364
AARG120
AARG73
ALYS270
site_idCSA2
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
BTHR328
BSER362
BGLU364
BARG120
BARG73
BLYS270
site_idCSA3
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
CTHR328
CSER362
CGLU364
CARG120
CARG73
CLYS270
site_idCSA4
Number of Residues6
DetailsAnnotated By Reference To The Literature 1pkn
ChainResidueDetails
DTHR328
DSER362
DGLU364
DARG120
DARG73
DLYS270

247536

PDB entries from 2026-01-14

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