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4B2D

human PKM2 with L-serine and FBP bound.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0003723molecular_functionRNA binding
A0003729molecular_functionmRNA binding
A0003824molecular_functioncatalytic activity
A0004713molecular_functionprotein tyrosine kinase activity
A0004743molecular_functionpyruvate kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
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
B0004713molecular_functionprotein tyrosine kinase activity
B0004743molecular_functionpyruvate kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
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
C0004713molecular_functionprotein tyrosine kinase activity
C0004743molecular_functionpyruvate kinase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005576cellular_componentextracellular region
C0005634cellular_componentnucleus
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
D0004713molecular_functionprotein tyrosine kinase activity
D0004743molecular_functionpyruvate kinase activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005576cellular_componentextracellular region
D0005634cellular_componentnucleus
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 PROSITE/UniProt
site_idPS00110
Number of Residues13
DetailsPYRUVATE_KINASE Pyruvate kinase active site signature. IkIISKIENhEGV
ChainResidueDetails
DILE265-VAL277
AILE265-VAL277

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:23064226
ChainResidueDetails
DASN70
DARG106
DHIS464
BASN70
BARG106
BHIS464
CASN70
CARG106
CHIS464

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P30613
ChainResidueDetails
DARG73
BTHR328
CARG73
CLYS270
CGLY295
CASP296
CTHR328
DLYS270
DGLY295
DASP296
DTHR328
BARG73
BLYS270
BGLY295
BASP296

site_idSWS_FT_FI3
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF
ChainResidueDetails
DASN75
BASP113
BTHR114
BARG120
BLYS207
BGLU272
CASN75
CSER77
CASP113
CTHR114
CARG120
DSER77
CLYS207
CGLU272
DASP113
DTHR114
DARG120
DLYS207
DGLU272
BASN75
BSER77

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:23530218, ECO:0007744|PDB:1T5A, ECO:0007744|PDB:4FXF
ChainResidueDetails
DTHR432
CTRP482
CARG489
CARG516
DTRP482
DARG489
DARG516
BTHR432
BTRP482
BARG489
BARG516
CTHR432

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:P00549
ChainResidueDetails
DLYS270
BLYS270
CLYS270

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Crucial for phosphotyrosine binding => ECO:0000269|PubMed:27199445
ChainResidueDetails
DLYS433
BLYS433
CLYS433

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0000269|Ref.11, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712
ChainResidueDetails
DSER2
BSER2
CSER2

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N6,N6,N6-trimethyllysine => ECO:0007744|PubMed:24129315
ChainResidueDetails
DLYS3
BLYS3
CLYS3

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
DSER37
BSER37
CSER37

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
DTHR41
BTHR41
CTHR41

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
DLYS62
DLYS89
BLYS62
BLYS89
CLYS62
CLYS89

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
DLYS66
DLYS498
BLYS66
BLYS498
CLYS66
CLYS498

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P11980
ChainResidueDetails
DSER97
DSER100
BSER97
BSER100
CSER97
CSER100

site_idSWS_FT_FI14
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:23186163
ChainResidueDetails
DTYR105
BTYR105
CTYR105

site_idSWS_FT_FI15
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
DSER127
BSER127
CSER127

site_idSWS_FT_FI16
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
DTYR148
BTYR148
CTYR148

site_idSWS_FT_FI17
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
DLYS166
DLYS322
BLYS166
BLYS322
CLYS166
CLYS322

site_idSWS_FT_FI18
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332
ChainResidueDetails
DTYR175
BTYR175
CTYR175

site_idSWS_FT_FI19
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332
ChainResidueDetails
DTHR195
BTHR195
CTHR195

site_idSWS_FT_FI20
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
DLYS266
BLYS266
CLYS266

site_idSWS_FT_FI21
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
DLYS270
BLYS270
CLYS270

site_idSWS_FT_FI22
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:21700219
ChainResidueDetails
DLYS305
BLYS305
CLYS305

site_idSWS_FT_FI23
Number of Residues2
DetailsMOD_RES: 4-hydroxyproline => ECO:0000269|PubMed:21620138
ChainResidueDetails
DPRO403
DPRO408
BPRO403
BPRO408
CPRO403
CPRO408

site_idSWS_FT_FI24
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:30487609
ChainResidueDetails
DCYS423
DCYS424
BCYS423
BCYS424
CCYS423
CCYS424

site_idSWS_FT_FI25
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:24120661, ECO:0000269|PubMed:26787900, ECO:0007744|PubMed:19608861
ChainResidueDetails
DLYS433
BLYS433
CLYS433

site_idSWS_FT_FI26
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
DLYS475
BLYS475
CLYS475

site_idSWS_FT_FI27
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
DLYS115
BLYS115
CLYS115

site_idSWS_FT_FI28
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
ChainResidueDetails
DLYS266
DLYS270
BLYS266
BLYS270
CLYS266
CLYS270

site_idSWS_FT_FI29
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate => ECO:0007744|PubMed:25114211
ChainResidueDetails
DLYS166
BLYS166
CLYS166

237423

PDB entries from 2025-06-11

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