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6WP4

Pyruvate Kinase M2 mutant-S37E

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 Residues9
Detailsbinding site for residue PO4 A 601
ChainResidue
ATHR432
ALYS433
ASER434
AARG436
ASER437
ASER519
AGLY520
AHOH708
AHOH716

site_idAC2
Number of Residues6
Detailsbinding site for residue PO4 A 602
ChainResidue
AHIS78
AGLY79
AHOH706
AHOH767
BTHR80
BHOH794

site_idAC3
Number of Residues4
Detailsbinding site for residue PO4 A 603
ChainResidue
AHIS274
AGLU275
AARG278
AHOH815

site_idAC4
Number of Residues5
Detailsbinding site for residue MG A 604
ChainResidue
AGLU272
AASP296
AOXL606
AHOH779
AHOH787

site_idAC5
Number of Residues5
Detailsbinding site for residue K A 605
ChainResidue
AASN75
ASER77
AASP113
ATHR114
AHOH783

site_idAC6
Number of Residues10
Detailsbinding site for residue OXL A 606
ChainResidue
ALYS270
AGLU272
AALA293
AARG294
AGLY295
AASP296
ATHR328
AMG604
AHOH779
AHOH787

site_idAC7
Number of Residues3
Detailsbinding site for residue GOL A 607
ChainResidue
AGLN227
APHE231
BGLU150

site_idAC8
Number of Residues9
Detailsbinding site for residue GOL A 608
ChainResidue
AILE88
ALYS89
AARG92
AHOH751
BGLY126
BGLY128
BTHR129
BALA130
BHOH727

site_idAC9
Number of Residues6
Detailsbinding site for residue GOL A 609
ChainResidue
AGLY126
AGLY128
AHOH710
AHOH744
BLYS89
BARG92

site_idAD1
Number of Residues7
Detailsbinding site for residue GOL A 610
ChainResidue
AARG43
AASN44
AASN70
AHIS464
AILE469
APHE470
AHOH702

site_idAD2
Number of Residues6
Detailsbinding site for residue GOL A 611
ChainResidue
APRO117
AASN210
ALEU211
AARG246
AGLU300
AHOH792

site_idAD3
Number of Residues6
Detailsbinding site for residue GOL A 612
ChainResidue
AGLU118
AILE119
AGLY208
AVAL209
APHE244
AASP296

site_idAD4
Number of Residues7
Detailsbinding site for residue PO4 B 601
ChainResidue
ATHR80
AHOH767
BHIS78
BGLY79
BHOH793
BHOH794
BHOH803

site_idAD5
Number of Residues7
Detailsbinding site for residue PO4 B 602
ChainResidue
BTHR432
BLYS433
BSER434
BSER437
BSER519
BGLY520
BHOH716

site_idAD6
Number of Residues4
Detailsbinding site for residue PO4 B 603
ChainResidue
BHIS274
BGLU275
BARG278
BHOH762

site_idAD7
Number of Residues4
Detailsbinding site for residue MG B 604
ChainResidue
BGLU272
BASP296
BHOH724
BHOH729

site_idAD8
Number of Residues6
Detailsbinding site for residue K B 605
ChainResidue
BSER77
BASP113
BTHR114
BHOH764
BHOH822
BASN75

site_idAD9
Number of Residues7
Detailsbinding site for residue GOL B 606
ChainResidue
BARG43
BASN44
BGLY46
BASN70
BHIS464
BILE469
BHOH701

site_idAE1
Number of Residues5
Detailsbinding site for residue GOL B 607
ChainResidue
BPRO117
BASN210
BLEU211
BVAL216
BGLU300

site_idAE2
Number of Residues5
Detailsbinding site for residue GOL B 608
ChainResidue
BARG399
BHOH723
CGLU418
CPHE421
CGOL609

site_idAE3
Number of Residues8
Detailsbinding site for residue PO4 C 601
ChainResidue
CTHR432
CLYS433
CSER434
CARG436
CSER437
CSER519
CGLY520
CHOH716

site_idAE4
Number of Residues3
Detailsbinding site for residue PO4 C 602
ChainResidue
CHIS78
CGLY79
CLYS206

site_idAE5
Number of Residues3
Detailsbinding site for residue MG C 603
ChainResidue
CGLU272
CASP296
CHOH828

site_idAE6
Number of Residues7
Detailsbinding site for residue K C 604
ChainResidue
CASN75
CSER77
CASP113
CTHR114
CSER243
CHOH743
CHOH819

site_idAE7
Number of Residues9
Detailsbinding site for residue GOL C 605
ChainResidue
CARG43
CASN44
CGLY46
CASN70
CHIS464
CTYR466
CILE469
CPHE470
CHOH713

site_idAE8
Number of Residues4
Detailsbinding site for residue GOL C 606
ChainResidue
CASN75
CHIS78
CARG120
CHOH819

site_idAE9
Number of Residues6
Detailsbinding site for residue GOL C 607
ChainResidue
CPRO117
CASN210
CLEU211
CGLU300
CGOL608
CHOH748

site_idAF1
Number of Residues7
Detailsbinding site for residue GOL C 608
ChainResidue
CGLU118
CILE119
CGLY208
CVAL209
CPHE244
CASP296
CGOL607

site_idAF2
Number of Residues3
Detailsbinding site for residue GOL C 609
ChainResidue
BGOL608
CHIS391
CPHE421

site_idAF3
Number of Residues2
Detailsbinding site for residue CL C 610
ChainResidue
CLYS247
CARG279

site_idAF4
Number of Residues1
Detailsbinding site for residue CL C 611
ChainResidue
CARG278

site_idAF5
Number of Residues8
Detailsbinding site for residue PO4 D 601
ChainResidue
DTHR432
DLYS433
DSER434
DARG436
DSER437
DSER519
DGLY520
DHOH760

site_idAF6
Number of Residues2
Detailsbinding site for residue PO4 D 602
ChainResidue
DHIS78
DARG120

site_idAF7
Number of Residues2
Detailsbinding site for residue PO4 D 603
ChainResidue
DHIS78
DGLY79

site_idAF8
Number of Residues5
Detailsbinding site for residue MG D 604
ChainResidue
DGLU272
DASP296
DOXL607
DHOH722
DHOH757

site_idAF9
Number of Residues6
Detailsbinding site for residue K D 605
ChainResidue
DASN75
DSER77
DASP113
DTHR114
DSER243
DHOH719

site_idAG1
Number of Residues1
Detailsbinding site for residue K D 606
ChainResidue
DASP236

site_idAG2
Number of Residues10
Detailsbinding site for residue OXL D 607
ChainResidue
DLYS270
DGLU272
DALA293
DARG294
DGLY295
DASP296
DTHR328
DMG604
DHOH722
DHOH757

site_idAG3
Number of Residues6
Detailsbinding site for residue GOL D 608
ChainResidue
DARG43
DASN70
DHIS464
DILE469
DPHE470
DHOH713

site_idAG4
Number of Residues5
Detailsbinding site for residue GOL D 609
ChainResidue
DTHR50
DARG73
DASN75
DSER362
DGLY363

site_idAG5
Number of Residues6
Detailsbinding site for residue GOL D 610
ChainResidue
DPRO117
DVAL209
DASN210
DLEU211
DGLU300
DHOH717

site_idAG6
Number of Residues1
Detailsbinding site for residue GOL D 611
ChainResidue
DHIS274

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 Residues672
DetailsRegion: {"description":"Interaction with POU5F1","evidences":[{"source":"PubMed","id":"18191611","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues176
DetailsRegion: {"description":"Intersubunit contact"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"23064226","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P30613","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues40
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"23530218","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4FXF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues43
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_FI7
Number of Residues4
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P00549","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsSite: {"description":"Crucial for phosphotyrosine binding","evidences":[{"source":"PubMed","id":"27199445","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
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_FI10
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues8
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues8
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues8
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P11980","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
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_FI15
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues8
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"21700219","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues8
DetailsModified residue: {"description":"4-hydroxyproline","evidences":[{"source":"PubMed","id":"21620138","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI24
Number of Residues8
DetailsModified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"30487609","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI25
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_FI26
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI27
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_FI28
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_FI29
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

247536

PDB entries from 2026-01-14

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