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4FXF

Structure of M2 pyruvate kinase in complex with phenylalanine

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0003723molecular_functionRNA binding
A0003729molecular_functionmRNA binding
A0003824molecular_functioncatalytic 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
A0006338biological_processchromatin remodeling
A0006417biological_processregulation of translation
A0012501biological_processprogrammed cell death
A0016301molecular_functionkinase activity
A0023026molecular_functionMHC class II protein complex binding
A0030955molecular_functionpotassium ion binding
A0031982cellular_componentvesicle
A0032869biological_processcellular response to insulin stimulus
A0034774cellular_componentsecretory granule lumen
A0035401molecular_functionhistone H3Y41 kinase activity
A0045296molecular_functioncadherin binding
A0046872molecular_functionmetal ion binding
A0061621biological_processcanonical glycolysis
A0062023cellular_componentcollagen-containing extracellular matrix
A0070062cellular_componentextracellular exosome
A0140801molecular_functionhistone H2AXY142 kinase activity
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
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
B0006338biological_processchromatin remodeling
B0006417biological_processregulation of translation
B0012501biological_processprogrammed cell death
B0016301molecular_functionkinase activity
B0023026molecular_functionMHC class II protein complex binding
B0030955molecular_functionpotassium ion binding
B0031982cellular_componentvesicle
B0032869biological_processcellular response to insulin stimulus
B0034774cellular_componentsecretory granule lumen
B0035401molecular_functionhistone H3Y41 kinase activity
B0045296molecular_functioncadherin binding
B0046872molecular_functionmetal ion binding
B0061621biological_processcanonical glycolysis
B0062023cellular_componentcollagen-containing extracellular matrix
B0070062cellular_componentextracellular exosome
B0140801molecular_functionhistone H2AXY142 kinase activity
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
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
C0006338biological_processchromatin remodeling
C0006417biological_processregulation of translation
C0012501biological_processprogrammed cell death
C0016301molecular_functionkinase activity
C0023026molecular_functionMHC class II protein complex binding
C0030955molecular_functionpotassium ion binding
C0031982cellular_componentvesicle
C0032869biological_processcellular response to insulin stimulus
C0034774cellular_componentsecretory granule lumen
C0035401molecular_functionhistone H3Y41 kinase activity
C0045296molecular_functioncadherin binding
C0046872molecular_functionmetal ion binding
C0061621biological_processcanonical glycolysis
C0062023cellular_componentcollagen-containing extracellular matrix
C0070062cellular_componentextracellular exosome
C0140801molecular_functionhistone H2AXY142 kinase activity
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
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
D0006338biological_processchromatin remodeling
D0006417biological_processregulation of translation
D0012501biological_processprogrammed cell death
D0016301molecular_functionkinase activity
D0023026molecular_functionMHC class II protein complex binding
D0030955molecular_functionpotassium ion binding
D0031982cellular_componentvesicle
D0032869biological_processcellular response to insulin stimulus
D0034774cellular_componentsecretory granule lumen
D0035401molecular_functionhistone H3Y41 kinase activity
D0045296molecular_functioncadherin binding
D0046872molecular_functionmetal ion binding
D0061621biological_processcanonical glycolysis
D0062023cellular_componentcollagen-containing extracellular matrix
D0070062cellular_componentextracellular exosome
D0140801molecular_functionhistone H2AXY142 kinase activity
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
AILE265-VAL277

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:23064226
ChainResidueDetails
AASN70
BASN70
BARG106
BHIS464
AARG106
AHIS464
DASN70
DARG106
DHIS464
CASN70
CARG106
CHIS464

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

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

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
BTHR432
BTRP482
BARG489
BARG516
ATRP482
AARG489
AARG516
DTHR432
DTRP482
DARG489
DARG516
CTHR432

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

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

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
DSER2
CSER2
BSER2

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

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
DSER37
CSER37
BSER37

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

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

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

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

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

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

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

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

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

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

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

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

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

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

site_idSWS_FT_FI24
Number of Residues8
DetailsMOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:30487609
ChainResidueDetails
ACYS423
ACYS424
DCYS423
DCYS424
CCYS423
CCYS424
BCYS423
BCYS424

site_idSWS_FT_FI25
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:24120661, ECO:0000269|PubMed:26787900, ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS433
DLYS433
CLYS433
BLYS433

site_idSWS_FT_FI26
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
ALYS475
DLYS475
CLYS475
BLYS475

site_idSWS_FT_FI27
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS115
DLYS115
CLYS115
BLYS115

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
BLYS266
BLYS270
ALYS266
ALYS270
DLYS266
DLYS270
CLYS266
CLYS270

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
ALYS166
DLYS166
CLYS166
BLYS166

227111

PDB entries from 2024-11-06

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