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

3SRF

Human M1 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
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
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
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
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
E0000287molecular_functionmagnesium ion binding
E0003723molecular_functionRNA binding
E0003729molecular_functionmRNA binding
E0003824molecular_functioncatalytic activity
E0004713molecular_functionprotein tyrosine kinase activity
E0004743molecular_functionpyruvate kinase activity
E0005515molecular_functionprotein binding
E0005524molecular_functionATP binding
E0005576cellular_componentextracellular region
E0005634cellular_componentnucleus
E0005737cellular_componentcytoplasm
E0005739cellular_componentmitochondrion
E0005791cellular_componentrough endoplasmic reticulum
E0005829cellular_componentcytosol
E0005929cellular_componentcilium
E0006096biological_processglycolytic process
E0006417biological_processregulation of translation
E0012501biological_processprogrammed cell death
E0016301molecular_functionkinase activity
E0023026molecular_functionMHC class II protein complex binding
E0030955molecular_functionpotassium ion binding
E0031982cellular_componentvesicle
E0032869biological_processcellular response to insulin stimulus
E0034774cellular_componentsecretory granule lumen
E0045296molecular_functioncadherin binding
E0046872molecular_functionmetal ion binding
E0061621biological_processcanonical glycolysis
E0062023cellular_componentcollagen-containing extracellular matrix
E0070062cellular_componentextracellular exosome
E1903561cellular_componentextracellular vesicle
E1903672biological_processpositive regulation of sprouting angiogenesis
E1904813cellular_componentficolin-1-rich granule lumen
E2000767biological_processpositive regulation of cytoplasmic translation
F0000287molecular_functionmagnesium ion binding
F0003723molecular_functionRNA binding
F0003729molecular_functionmRNA binding
F0003824molecular_functioncatalytic activity
F0004713molecular_functionprotein tyrosine kinase activity
F0004743molecular_functionpyruvate kinase activity
F0005515molecular_functionprotein binding
F0005524molecular_functionATP binding
F0005576cellular_componentextracellular region
F0005634cellular_componentnucleus
F0005737cellular_componentcytoplasm
F0005739cellular_componentmitochondrion
F0005791cellular_componentrough endoplasmic reticulum
F0005829cellular_componentcytosol
F0005929cellular_componentcilium
F0006096biological_processglycolytic process
F0006417biological_processregulation of translation
F0012501biological_processprogrammed cell death
F0016301molecular_functionkinase activity
F0023026molecular_functionMHC class II protein complex binding
F0030955molecular_functionpotassium ion binding
F0031982cellular_componentvesicle
F0032869biological_processcellular response to insulin stimulus
F0034774cellular_componentsecretory granule lumen
F0045296molecular_functioncadherin binding
F0046872molecular_functionmetal ion binding
F0061621biological_processcanonical glycolysis
F0062023cellular_componentcollagen-containing extracellular matrix
F0070062cellular_componentextracellular exosome
F1903561cellular_componentextracellular vesicle
F1903672biological_processpositive regulation of sprouting angiogenesis
F1904813cellular_componentficolin-1-rich granule lumen
F2000767biological_processpositive regulation of cytoplasmic translation
G0000287molecular_functionmagnesium ion binding
G0003723molecular_functionRNA binding
G0003729molecular_functionmRNA binding
G0003824molecular_functioncatalytic activity
G0004713molecular_functionprotein tyrosine kinase activity
G0004743molecular_functionpyruvate kinase activity
G0005515molecular_functionprotein binding
G0005524molecular_functionATP binding
G0005576cellular_componentextracellular region
G0005634cellular_componentnucleus
G0005737cellular_componentcytoplasm
G0005739cellular_componentmitochondrion
G0005791cellular_componentrough endoplasmic reticulum
G0005829cellular_componentcytosol
G0005929cellular_componentcilium
G0006096biological_processglycolytic process
G0006417biological_processregulation of translation
G0012501biological_processprogrammed cell death
G0016301molecular_functionkinase activity
G0023026molecular_functionMHC class II protein complex binding
G0030955molecular_functionpotassium ion binding
G0031982cellular_componentvesicle
G0032869biological_processcellular response to insulin stimulus
G0034774cellular_componentsecretory granule lumen
G0045296molecular_functioncadherin binding
G0046872molecular_functionmetal ion binding
G0061621biological_processcanonical glycolysis
G0062023cellular_componentcollagen-containing extracellular matrix
G0070062cellular_componentextracellular exosome
G1903561cellular_componentextracellular vesicle
G1903672biological_processpositive regulation of sprouting angiogenesis
G1904813cellular_componentficolin-1-rich granule lumen
G2000767biological_processpositive regulation of cytoplasmic translation
H0000287molecular_functionmagnesium ion binding
H0003723molecular_functionRNA binding
H0003729molecular_functionmRNA binding
H0003824molecular_functioncatalytic activity
H0004713molecular_functionprotein tyrosine kinase activity
H0004743molecular_functionpyruvate kinase activity
H0005515molecular_functionprotein binding
H0005524molecular_functionATP binding
H0005576cellular_componentextracellular region
H0005634cellular_componentnucleus
H0005737cellular_componentcytoplasm
H0005739cellular_componentmitochondrion
H0005791cellular_componentrough endoplasmic reticulum
H0005829cellular_componentcytosol
H0005929cellular_componentcilium
H0006096biological_processglycolytic process
H0006417biological_processregulation of translation
H0012501biological_processprogrammed cell death
H0016301molecular_functionkinase activity
H0023026molecular_functionMHC class II protein complex binding
H0030955molecular_functionpotassium ion binding
H0031982cellular_componentvesicle
H0032869biological_processcellular response to insulin stimulus
H0034774cellular_componentsecretory granule lumen
H0045296molecular_functioncadherin binding
H0046872molecular_functionmetal ion binding
H0061621biological_processcanonical glycolysis
H0062023cellular_componentcollagen-containing extracellular matrix
H0070062cellular_componentextracellular exosome
H1903561cellular_componentextracellular vesicle
H1903672biological_processpositive regulation of sprouting angiogenesis
H1904813cellular_componentficolin-1-rich granule lumen
H2000767biological_processpositive regulation of cytoplasmic translation
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 C 531
ChainResidue
CTHR431
CGLU432
CSER433
CGLY434
CARG435
CSER436
CGLY519

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K C 532
ChainResidue
CASP112
CTHR113
CSER242
CLYS269
CASN74
CSER76

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG C 533
ChainResidue
CGLU271
CASP295
CPYR534

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PYR C 534
ChainResidue
CARG72
CLYS269
CGLU271
CMET290
CALA292
CGLY294
CASP295
CTHR327
CSER361
CMG533

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL C 535
ChainResidue
CARG42
CASN43
CHIS463
CTYR465
CILE468
CPHE469

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 A 531
ChainResidue
ATHR431
AGLU432
ASER433
AGLY434
AARG435
ASER436
AGLY519
AHOH568
AHOH591

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K A 532
ChainResidue
AASN74
ASER76
AASP112
ATHR113
AHOH551
AHOH594

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 533
ChainResidue
AGLU271
AASP295
APYR534

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PYR A 534
ChainResidue
ALYS269
AGLU271
AALA292
AARG293
AGLY294
AASP295
ATHR327
AMG533
AHOH594

site_idBC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 535
ChainResidue
AARG42
AASN43
AGLY45
AASN69
AHIS463
AILE468
APHE469
APRO470

site_idBC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 B 531
ChainResidue
BTHR431
BGLU432
BSER433
BGLY434
BARG435
BSER436
BGLY519
BPHE520

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K B 532
ChainResidue
BASN74
BSER76
BASP112
BTHR113
BLYS269

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 533
ChainResidue
BGLU271
BASP295
BPYR534

site_idBC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PYR B 534
ChainResidue
BLYS269
BGLU271
BMET290
BALA292
BGLY294
BASP295
BTHR327
BMG533

site_idBC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL B 535
ChainResidue
BARG42
BASN43
BTHR44
BGLY45
BASN69
BHIS463
BILE468
BPHE469

site_idBC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 D 531
ChainResidue
DLEU430
DTHR431
DGLU432
DSER433
DGLY434
DARG435
DSER436
DGLY519

site_idBC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K D 532
ChainResidue
DASN74
DSER76
DASP112
DTHR113
DLYS269
DHOH556

site_idBC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG D 533
ChainResidue
DGLU271
DASP295
DPYR534
DHOH556

site_idCC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PYR D 534
ChainResidue
DLYS269
DGLU271
DALA292
DGLY294
DASP295
DTHR327
DMG533

site_idCC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL D 535
ChainResidue
DARG42
DASN43
DGLY45
DASN69
DHIS463
DILE468
DPHE469

site_idCC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 E 531
ChainResidue
ELEU430
ETHR431
EGLU432
ESER433
EGLY434
EARG435
ESER436
EGLY519

site_idCC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K E 532
ChainResidue
EASN74
ESER76
ETHR113
ELYS269

site_idCC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG E 533
ChainResidue
ELYS269
EGLU271
EASP295
EPYR534

site_idCC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PYR E 534
ChainResidue
ELYS269
EGLU271
EALA292
EGLY294
EASP295
ETHR327
EMG533

site_idCC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL E 535
ChainResidue
EARG42
EASN43
ETHR44
EGLY45
EASN69
EHIS463
EILE468
EPHE469

site_idCC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 F 531
ChainResidue
FTHR431
FGLU432
FSER433
FGLY434
FARG435
FSER436
FGLY519
FPHE520
FHOH578

site_idCC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K F 532
ChainResidue
FASN74
FSER76
FASP112
FTHR113
FLYS269
FHOH581

site_idDC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG F 533
ChainResidue
FGLU271
FASP295
FPYR534

site_idDC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PYR F 534
ChainResidue
FLYS269
FGLU271
FALA292
FGLY294
FASP295
FTHR327
FMG533

site_idDC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL F 535
ChainResidue
FPRO116
FASN209
FLEU210
FVAL215
FGLU299

site_idDC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL F 536
ChainResidue
FARG42
FASN43
FGLY45
FASN69
FHIS463
FTYR465
FILE468
FPHE469

site_idDC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 G 531
ChainResidue
GLEU430
GTHR431
GGLU432
GSER433
GGLY434
GARG435
GSER436
GGLY519

site_idDC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE K G 532
ChainResidue
GASN74
GSER76
GASP112
GTHR113
GSER242
GLYS269
GHOH585

site_idDC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG G 533
ChainResidue
GGLU271
GASP295
GPYR534
GHOH584

site_idDC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PYR G 534
ChainResidue
GARG72
GLYS269
GGLU271
GALA292
GGLY294
GASP295
GTHR327
GMG533
GHOH585

site_idDC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL G 535
ChainResidue
GARG42
GASN43
GGLY45
GASN69
GHIS463
GTYR465
GILE468
GPHE469

site_idEC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 H 531
ChainResidue
HTHR431
HGLU432
HSER433
HARG435
HSER436

site_idEC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K H 532
ChainResidue
HASN74
HSER76
HASP112
HTHR113
HLYS269

site_idEC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG H 533
ChainResidue
HLYS269
HGLU271
HASP295
HPYR534

site_idEC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PYR H 534
ChainResidue
HMET290
HALA292
HGLY294
HASP295
HTHR327
HMG533

Functional Information from PROSITE/UniProt
site_idPS00110
Number of Residues13
DetailsPYRUVATE_KINASE Pyruvate kinase active site signature. IkIISKIENhEGV
ChainResidueDetails
CILE264-VAL276

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:23064226
ChainResidueDetails
CASN69
DASN69
DARG105
DHIS463
EASN69
EARG105
EHIS463
FASN69
FARG105
FHIS463
GASN69
CARG105
GARG105
GHIS463
HASN69
HARG105
HHIS463
CHIS463
AASN69
AARG105
AHIS463
BASN69
BARG105
BHIS463

site_idSWS_FT_FI2
Number of Residues40
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P30613
ChainResidueDetails
CARG72
ATHR327
BARG72
BLYS269
BGLY294
BASP295
BTHR327
DARG72
DLYS269
DGLY294
DASP295
CLYS269
DTHR327
EARG72
ELYS269
EGLY294
EASP295
ETHR327
FARG72
FLYS269
FGLY294
FASP295
CGLY294
FTHR327
GARG72
GLYS269
GGLY294
GASP295
GTHR327
HARG72
HLYS269
HGLY294
HASP295
CASP295
HTHR327
CTHR327
AARG72
ALYS269
AGLY294
AASP295

site_idSWS_FT_FI3
Number of Residues56
DetailsBINDING: BINDING => ECO:0000269|PubMed:23530218, ECO:0007744|PDB:4FXF
ChainResidueDetails
CASN74
AASP112
ATHR113
AARG119
ALYS206
AGLU271
BASN74
BSER76
BASP112
BTHR113
BARG119
CSER76
BLYS206
BGLU271
DASN74
DSER76
DASP112
DTHR113
DARG119
DLYS206
DGLU271
EASN74
CASP112
ESER76
EASP112
ETHR113
EARG119
ELYS206
EGLU271
FASN74
FSER76
FASP112
FTHR113
CTHR113
FARG119
FLYS206
FGLU271
GASN74
GSER76
GASP112
GTHR113
GARG119
GLYS206
GGLU271
CARG119
HASN74
HSER76
HASP112
HTHR113
HARG119
HLYS206
HGLU271
CLYS206
CGLU271
AASN74
ASER76

site_idSWS_FT_FI4
Number of Residues32
DetailsBINDING: BINDING => ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:23530218, ECO:0007744|PDB:1T5A, ECO:0007744|PDB:4FXF
ChainResidueDetails
CTHR431
BTRP481
BARG488
BARG515
DTHR431
DTRP481
DARG488
DARG515
ETHR431
ETRP481
EARG488
CTRP481
EARG515
FTHR431
FTRP481
FARG488
FARG515
GTHR431
GTRP481
GARG488
GARG515
HTHR431
CARG488
HTRP481
HARG488
HARG515
CARG515
ATHR431
ATRP481
AARG488
AARG515
BTHR431

site_idSWS_FT_FI5
Number of Residues8
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:P00549
ChainResidueDetails
CLYS269
ALYS269
BLYS269
DLYS269
ELYS269
FLYS269
GLYS269
HLYS269

site_idSWS_FT_FI6
Number of Residues8
DetailsSITE: Crucial for phosphotyrosine binding => ECO:0000269|PubMed:27199445
ChainResidueDetails
CGLU432
AGLU432
BGLU432
DGLU432
EGLU432
FGLU432
GGLU432
HGLU432

site_idSWS_FT_FI7
Number of Residues8
DetailsMOD_RES: N-acetylserine => ECO:0000269|Ref.11, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712
ChainResidueDetails
CSER1
ASER1
BSER1
DSER1
ESER1
FSER1
GSER1
HSER1

site_idSWS_FT_FI8
Number of Residues8
DetailsMOD_RES: N6,N6,N6-trimethyllysine => ECO:0007744|PubMed:24129315
ChainResidueDetails
CLYS2
ALYS2
BLYS2
DLYS2
ELYS2
FLYS2
GLYS2
HLYS2

site_idSWS_FT_FI9
Number of Residues8
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
CSER36
ASER36
BSER36
DSER36
ESER36
FSER36
GSER36
HSER36

site_idSWS_FT_FI10
Number of Residues8
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
CTHR40
ATHR40
BTHR40
DTHR40
ETHR40
FTHR40
GTHR40
HTHR40

site_idSWS_FT_FI11
Number of Residues16
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
CLYS61
ELYS88
FLYS61
FLYS88
GLYS61
GLYS88
HLYS61
HLYS88
CLYS88
ALYS61
ALYS88
BLYS61
BLYS88
DLYS61
DLYS88
ELYS61

site_idSWS_FT_FI12
Number of Residues16
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
CLYS65
ELYS497
FLYS65
FLYS497
GLYS65
GLYS497
HLYS65
HLYS497
CLYS497
ALYS65
ALYS497
BLYS65
BLYS497
DLYS65
DLYS497
ELYS65

site_idSWS_FT_FI13
Number of Residues16
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P11980
ChainResidueDetails
CSER96
ESER99
FSER96
FSER99
GSER96
GSER99
HSER96
HSER99
CSER99
ASER96
ASER99
BSER96
BSER99
DSER96
DSER99
ESER96

site_idSWS_FT_FI14
Number of Residues8
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:23186163
ChainResidueDetails
CTYR104
ATYR104
BTYR104
DTYR104
ETYR104
FTYR104
GTYR104
HTYR104

site_idSWS_FT_FI15
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
CSER126
ASER126
BSER126
DSER126
ESER126
FSER126
GSER126
HSER126

site_idSWS_FT_FI16
Number of Residues8
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
CTYR147
ATYR147
BTYR147
DTYR147
ETYR147
FTYR147
GTYR147
HTYR147

site_idSWS_FT_FI17
Number of Residues16
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
CLYS165
ELYS321
FLYS165
FLYS321
GLYS165
GLYS321
HLYS165
HLYS321
CLYS321
ALYS165
ALYS321
BLYS165
BLYS321
DLYS165
DLYS321
ELYS165

site_idSWS_FT_FI18
Number of Residues8
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332
ChainResidueDetails
CTYR174
ATYR174
BTYR174
DTYR174
ETYR174
FTYR174
GTYR174
HTYR174

site_idSWS_FT_FI19
Number of Residues8
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332
ChainResidueDetails
CTHR194
ATHR194
BTHR194
DTHR194
ETHR194
FTHR194
GTHR194
HTHR194

site_idSWS_FT_FI20
Number of Residues8
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
CLYS265
ALYS265
BLYS265
DLYS265
ELYS265
FLYS265
GLYS265
HLYS265

site_idSWS_FT_FI21
Number of Residues8
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
CLYS269
ALYS269
BLYS269
DLYS269
ELYS269
FLYS269
GLYS269
HLYS269

site_idSWS_FT_FI22
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:21700219
ChainResidueDetails
CLYS304
ALYS304
BLYS304
DLYS304
ELYS304
FLYS304
GLYS304
HLYS304

site_idSWS_FT_FI23
Number of Residues16
DetailsMOD_RES: 4-hydroxyproline => ECO:0000269|PubMed:21620138
ChainResidueDetails
CSER402
ELEU407
FSER402
FLEU407
GSER402
GLEU407
HSER402
HLEU407
CLEU407
ASER402
ALEU407
BSER402
BLEU407
DSER402
DLEU407
ESER402

site_idSWS_FT_FI24
Number of Residues16
DetailsMOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:30487609
ChainResidueDetails
CCYS422
ELEU423
FCYS422
FLEU423
GCYS422
GLEU423
HCYS422
HLEU423
CLEU423
ACYS422
ALEU423
BCYS422
BLEU423
DCYS422
DLEU423
ECYS422

site_idSWS_FT_FI25
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:24120661, ECO:0000269|PubMed:26787900, ECO:0007744|PubMed:19608861
ChainResidueDetails
CGLU432
AGLU432
BGLU432
DGLU432
EGLU432
FGLU432
GGLU432
HGLU432

site_idSWS_FT_FI26
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P52480
ChainResidueDetails
CLYS474
ALYS474
BLYS474
DLYS474
ELYS474
FLYS474
GLYS474
HLYS474

site_idSWS_FT_FI27
Number of Residues8
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
CLYS114
ALYS114
BLYS114
DLYS114
ELYS114
FLYS114
GLYS114
HLYS114

site_idSWS_FT_FI28
Number of Residues24
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
ChainResidueDetails
DLYS265
DLYS269
ELYS265
ELYS269
FLYS265
FLYS269
CLYS265
GLYS265
GLYS269
HLYS265
HLYS269
CLYS269
ALYS265
ALYS269
BLYS265
BLYS269

site_idSWS_FT_FI29
Number of Residues8
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate => ECO:0007744|PubMed:25114211
ChainResidueDetails
CLYS165
ALYS165
BLYS165
DLYS165
ELYS165
FLYS165
GLYS165
HLYS165

222036

PDB entries from 2024-07-03

PDB statisticsPDBj update infoContact PDBjnumon