Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4QGC

crystal structure of PKM2-K422R mutant

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
A0008152biological_processmetabolic process
A0012501biological_processprogrammed cell death
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
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
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
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
B0008152biological_processmetabolic process
B0012501biological_processprogrammed cell death
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
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
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
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
C0008152biological_processmetabolic process
C0012501biological_processprogrammed cell death
C0016301molecular_functionkinase activity
C0016310biological_processphosphorylation
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
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
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
D0008152biological_processmetabolic process
D0012501biological_processprogrammed cell death
D0016301molecular_functionkinase activity
D0016310biological_processphosphorylation
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
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 K A 1001
ChainResidue
AASN75
ASER77
AASP113
ATHR114
AHOH1102
AHOH1132

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1002
ChainResidue
ALYS433
ATRP482
AARG489

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 1003
ChainResidue
ATHR432
ALYS433
ASER434
AGLY435
AARG436
ASER437
ATHR522
AHOH1142

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1004
ChainResidue
AASN75
AHIS78
AARG120
AHOH1132
AHOH1169
AHOH1223

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 1005
ChainResidue
AARG43
AASN44
AASN70
AARG106
AHIS464
APHE470
AHOH1225
AHOH1237
AHOH1241

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K B 1001
ChainResidue
BASN75
BSER77
BASP113
BTHR114

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 1002
ChainResidue
BTHR432
BLYS433
BSER434
BGLY435
BARG436
BSER437

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1003
ChainResidue
BLYS433
BTRP482
BARG489
BHOH1153

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL B 1004
ChainResidue
BARG43
BASN44
BASN70
BHIS464
BTYR466
BILE469
BPRO471

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K C 1001
ChainResidue
CASN75
CSER77
CASP113
CTHR114
CHOH1101

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 1002
ChainResidue
CTHR432
CLYS433
CSER434
CARG436
CSER437
CHOH1180

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 C 1003
ChainResidue
CTRP482
CARG489
CGLY518

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL C 1004
ChainResidue
CARG43
CHIS464
CILE469

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K D 1001
ChainResidue
DASN75
DSER77
DASP113
DTHR114
DHOH1107

site_idBC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 D 1002
ChainResidue
DLYS433
DTRP482
DARG489

site_idBC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 D 1003
ChainResidue
DTHR432
DLYS433
DSER434
DARG436
DSER437
DHOH1128

site_idBC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL D 1004
ChainResidue
DARG43
DASN44
DASN70
DARG106
DHIS464
DILE469
DPHE470
DHOH1102
DHOH1169

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: BINDING => ECO:0000269|PubMed:23064226
ChainResidueDetails
AASN70
DASN70
DARG106
DHIS464
AARG106
AHIS464
BASN70
BARG106
BHIS464
CASN70
CARG106
CHIS464

site_idSWS_FT_FI2
Number of Residues20
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P30613
ChainResidueDetails
AARG73
BTHR328
CARG73
CLYS270
CGLY295
CASP296
CTHR328
DARG73
DLYS270
DGLY295
DASP296
ALYS270
DTHR328
AGLY295
AASP296
ATHR328
BARG73
BLYS270
BGLY295
BASP296

site_idSWS_FT_FI3
Number of Residues28
DetailsBINDING: BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF
ChainResidueDetails
AASN75
BASP113
BTHR114
BARG120
BLYS207
BGLU272
CASN75
CSER77
CASP113
CTHR114
CARG120
ASER77
CLYS207
CGLU272
DASN75
DSER77
DASP113
DTHR114
DARG120
DLYS207
DGLU272
AASP113
ATHR114
AARG120
ALYS207
AGLU272
BASN75
BSER77

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
ATHR432
CTRP482
CARG489
CARG516
DTHR432
DTRP482
DARG489
DARG516
ATRP482
AARG489
AARG516
BTHR432
BTRP482
BARG489
BARG516
CTHR432

site_idSWS_FT_FI5
Number of Residues4
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:P00549
ChainResidueDetails
ALYS270
BLYS270
CLYS270
DLYS270

site_idSWS_FT_FI6
Number of Residues4
DetailsSITE: Crucial for phosphotyrosine binding => ECO:0000269|PubMed:27199445
ChainResidueDetails
ALYS433
BLYS433
CLYS433
DLYS433

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: N-acetylserine => ECO:0000269|Ref.11, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712
ChainResidueDetails
ASER2
BSER2
CSER2
DSER2

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: N6,N6,N6-trimethyllysine => ECO:0007744|PubMed:24129315
ChainResidueDetails
ALYS3
BLYS3
CLYS3
DLYS3

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
ASER37
BSER37
CSER37
DSER37

site_idSWS_FT_FI10
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATHR41
BTHR41
CTHR41
DTHR41

site_idSWS_FT_FI11
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS62
ALYS89
BLYS62
BLYS89
CLYS62
CLYS89
DLYS62
DLYS89

site_idSWS_FT_FI12
Number of Residues8
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
ALYS66
ALYS498
BLYS66
BLYS498
CLYS66
CLYS498
DLYS66
DLYS498

site_idSWS_FT_FI13
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P11980
ChainResidueDetails
ASER97
ASER100
BSER97
BSER100
CSER97
CSER100
DSER97
DSER100

site_idSWS_FT_FI14
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:23186163
ChainResidueDetails
ATYR105
BTYR105
CTYR105
DTYR105

site_idSWS_FT_FI15
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER127
BSER127
CSER127
DSER127

site_idSWS_FT_FI16
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
ATYR148
BTYR148
CTYR148
DTYR148

site_idSWS_FT_FI17
Number of Residues8
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
ALYS166
ALYS322
BLYS166
BLYS322
CLYS166
CLYS322
DLYS166
DLYS322

site_idSWS_FT_FI18
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332
ChainResidueDetails
ATYR175
BTYR175
CTYR175
DTYR175

site_idSWS_FT_FI19
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332
ChainResidueDetails
ATHR195
BTHR195
CTHR195
DTHR195

site_idSWS_FT_FI20
Number of Residues4
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS266
BLYS266
CLYS266
DLYS266

site_idSWS_FT_FI21
Number of Residues4
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
ALYS270
BLYS270
CLYS270
DLYS270

site_idSWS_FT_FI22
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:21700219
ChainResidueDetails
ALYS305
BLYS305
CLYS305
DLYS305

site_idSWS_FT_FI23
Number of Residues8
DetailsMOD_RES: 4-hydroxyproline => ECO:0000269|PubMed:21620138
ChainResidueDetails
APRO403
APRO408
BPRO403
BPRO408
CPRO403
CPRO408
DPRO403
DPRO408

site_idSWS_FT_FI24
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:24120661, ECO:0000269|PubMed:26787900, ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS433
BLYS433
CLYS433
DLYS433

site_idSWS_FT_FI25
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
ALYS475
BLYS475
CLYS475
DLYS475

site_idSWS_FT_FI26
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS115
BLYS115
CLYS115
DLYS115

site_idSWS_FT_FI27
Number of Residues12
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
ChainResidueDetails
DLYS266
DLYS270
ALYS266
ALYS270
BLYS266
BLYS270
CLYS266
CLYS270

site_idSWS_FT_FI28
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate => ECO:0007744|PubMed:25114211
ChainResidueDetails
ALYS166
BLYS166
CLYS166
DLYS166

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon