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3SRH

Human M2 pyruvate kinase

Functional Information from GO Data
ChainGOidnamespacecontents
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
A0016310biological_processphosphorylation
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
A0062023cellular_componentcollagen-containing extracellular matrix
A0070062cellular_componentextracellular exosome
A1903561cellular_componentextracellular vesicle
A1903672biological_processpositive regulation of sprouting angiogenesis
A1904813cellular_componentficolin-1-rich granule lumen
A2000767biological_processpositive regulation of cytoplasmic translation
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
B0016310biological_processphosphorylation
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
B0062023cellular_componentcollagen-containing extracellular matrix
B0070062cellular_componentextracellular exosome
B1903561cellular_componentextracellular vesicle
B1903672biological_processpositive regulation of sprouting angiogenesis
B1904813cellular_componentficolin-1-rich granule lumen
B2000767biological_processpositive regulation of cytoplasmic translation
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
C0016310biological_processphosphorylation
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
C0062023cellular_componentcollagen-containing extracellular matrix
C0070062cellular_componentextracellular exosome
C1903561cellular_componentextracellular vesicle
C1903672biological_processpositive regulation of sprouting angiogenesis
C1904813cellular_componentficolin-1-rich granule lumen
C2000767biological_processpositive regulation of cytoplasmic translation
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
D0016310biological_processphosphorylation
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
D0062023cellular_componentcollagen-containing extracellular matrix
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 Residues6
DetailsBINDING SITE FOR RESIDUE PO4 A 531
ChainResidue
ATHR431
ALYS432
ASER433
ASER436
ASER518
AGLY519

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 B 531
ChainResidue
BGLY434
BARG435
BSER436
BSER518
BGLY519
BTHR431
BLYS432
BSER433

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 D 531
ChainResidue
DTHR431
DLYS432
DSER433
DARG435
DSER436
DSER518
DGLY519

Functional Information from PROSITE/UniProt
site_idPS00110
Number of Residues13
DetailsPYRUVATE_KINASE Pyruvate kinase active site signature. IkIISKIENhEGV
ChainResidueDetails
AILE264-VAL276

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:23064226
ChainResidueDetails
AASN69
DASN69
DARG105
DHIS463
AARG105
AHIS463
BASN69
BARG105
BHIS463
CASN69
CARG105
CHIS463

site_idSWS_FT_FI2
Number of Residues20
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P30613
ChainResidueDetails
AARG72
BTHR327
CARG72
CLYS269
CGLY294
CASP295
CTHR327
DARG72
DLYS269
DGLY294
DASP295
ALYS269
DTHR327
AGLY294
AASP295
ATHR327
BARG72
BLYS269
BGLY294
BASP295

site_idSWS_FT_FI3
Number of Residues28
DetailsBINDING: BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF
ChainResidueDetails
AASN74
BASP112
BTHR113
BARG119
BLYS206
BGLU271
CASN74
CSER76
CASP112
CTHR113
CARG119
ASER76
CLYS206
CGLU271
DASN74
DSER76
DASP112
DTHR113
DARG119
DLYS206
DGLU271
AASP112
ATHR113
AARG119
ALYS206
AGLU271
BASN74
BSER76

site_idSWS_FT_FI4
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:23530218, ECO:0007744|PDB:1T5A, ECO:0007744|PDB:4FXF
ChainResidueDetails
ATHR431
CTRP481
CARG488
CARG515
DTHR431
DTRP481
DARG488
DARG515
ATRP481
AARG488
AARG515
BTHR431
BTRP481
BARG488
BARG515
CTHR431

site_idSWS_FT_FI5
Number of Residues4
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:P00549
ChainResidueDetails
ALYS269
BLYS269
CLYS269
DLYS269

site_idSWS_FT_FI6
Number of Residues4
DetailsSITE: Crucial for phosphotyrosine binding => ECO:0000269|PubMed:27199445
ChainResidueDetails
ALYS432
BLYS432
CLYS432
DLYS432

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: N-acetylserine => ECO:0000269|Ref.11, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712
ChainResidueDetails
ASER1
BSER1
CSER1
DSER1

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: N6,N6,N6-trimethyllysine => ECO:0007744|PubMed:24129315
ChainResidueDetails
ALYS2
BLYS2
CLYS2
DLYS2

site_idSWS_FT_FI9
Number of Residues4
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
ASER36
BSER36
CSER36
DSER36

site_idSWS_FT_FI10
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR40
BTHR40
CTHR40
DTHR40

site_idSWS_FT_FI11
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS61
ALYS88
BLYS61
BLYS88
CLYS61
CLYS88
DLYS61
DLYS88

site_idSWS_FT_FI12
Number of Residues8
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
ALYS65
ALYS497
BLYS65
BLYS497
CLYS65
CLYS497
DLYS65
DLYS497

site_idSWS_FT_FI13
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P11980
ChainResidueDetails
ASER96
ASER99
BSER96
BSER99
CSER96
CSER99
DSER96
DSER99

site_idSWS_FT_FI14
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:23186163
ChainResidueDetails
ATYR104
BTYR104
CTYR104
DTYR104

site_idSWS_FT_FI15
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER126
BSER126
CSER126
DSER126

site_idSWS_FT_FI16
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
ATYR147
BTYR147
CTYR147
DTYR147

site_idSWS_FT_FI17
Number of Residues8
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
ALYS165
ALYS321
BLYS165
BLYS321
CLYS165
CLYS321
DLYS165
DLYS321

site_idSWS_FT_FI18
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332
ChainResidueDetails
ATYR174
BTYR174
CTYR174
DTYR174

site_idSWS_FT_FI19
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332
ChainResidueDetails
ATHR194
BTHR194
CTHR194
DTHR194

site_idSWS_FT_FI20
Number of Residues4
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS265
BLYS265
CLYS265
DLYS265

site_idSWS_FT_FI21
Number of Residues4
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
ALYS269
BLYS269
CLYS269
DLYS269

site_idSWS_FT_FI22
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:21700219
ChainResidueDetails
ALYS304
BLYS304
CLYS304
DLYS304

site_idSWS_FT_FI23
Number of Residues8
DetailsMOD_RES: 4-hydroxyproline => ECO:0000269|PubMed:21620138
ChainResidueDetails
APRO402
APRO407
BPRO402
BPRO407
CPRO402
CPRO407
DPRO402
DPRO407

site_idSWS_FT_FI24
Number of Residues8
DetailsMOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:30487609
ChainResidueDetails
ACYS422
ACYS423
BCYS422
BCYS423
CCYS422
CCYS423
DCYS422
DCYS423

site_idSWS_FT_FI25
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:24120661, ECO:0000269|PubMed:26787900, ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS432
BLYS432
CLYS432
DLYS432

site_idSWS_FT_FI26
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
ALYS474
BLYS474
CLYS474
DLYS474

site_idSWS_FT_FI27
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS114
BLYS114
CLYS114
DLYS114

site_idSWS_FT_FI28
Number of Residues12
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
ChainResidueDetails
DLYS265
DLYS269
ALYS265
ALYS269
BLYS265
BLYS269
CLYS265
CLYS269

site_idSWS_FT_FI29
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate => ECO:0007744|PubMed:25114211
ChainResidueDetails
ALYS165
BLYS165
CLYS165
DLYS165

226707

PDB entries from 2024-10-30

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