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8F5T

Rabbit muscle pyruvate kinase in complex with sodium and magnesium

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0003729molecular_functionmRNA binding
A0003824molecular_functioncatalytic activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0004715molecular_functionnon-membrane spanning protein tyrosine kinase activity
A0004743molecular_functionpyruvate kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005791cellular_componentrough endoplasmic reticulum
A0006096biological_processglycolytic process
A0006417biological_processregulation of translation
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0030955molecular_functionpotassium ion binding
A0046872molecular_functionmetal ion binding
A1903672biological_processpositive regulation of sprouting angiogenesis
A2000767biological_processpositive regulation of cytoplasmic translation
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0003729molecular_functionmRNA binding
B0003824molecular_functioncatalytic activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0004715molecular_functionnon-membrane spanning protein tyrosine kinase activity
B0004743molecular_functionpyruvate kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005791cellular_componentrough endoplasmic reticulum
B0006096biological_processglycolytic process
B0006417biological_processregulation of translation
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0030955molecular_functionpotassium ion binding
B0046872molecular_functionmetal ion binding
B1903672biological_processpositive regulation of sprouting angiogenesis
B2000767biological_processpositive regulation of cytoplasmic translation
C0000166molecular_functionnucleotide binding
C0000287molecular_functionmagnesium ion binding
C0003729molecular_functionmRNA binding
C0003824molecular_functioncatalytic activity
C0004674molecular_functionprotein serine/threonine kinase activity
C0004713molecular_functionprotein tyrosine kinase activity
C0004715molecular_functionnon-membrane spanning protein tyrosine kinase activity
C0004743molecular_functionpyruvate kinase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005791cellular_componentrough endoplasmic reticulum
C0006096biological_processglycolytic process
C0006417biological_processregulation of translation
C0016301molecular_functionkinase activity
C0016740molecular_functiontransferase activity
C0030955molecular_functionpotassium ion binding
C0046872molecular_functionmetal ion binding
C1903672biological_processpositive regulation of sprouting angiogenesis
C2000767biological_processpositive regulation of cytoplasmic translation
D0000166molecular_functionnucleotide binding
D0000287molecular_functionmagnesium ion binding
D0003729molecular_functionmRNA binding
D0003824molecular_functioncatalytic activity
D0004674molecular_functionprotein serine/threonine kinase activity
D0004713molecular_functionprotein tyrosine kinase activity
D0004715molecular_functionnon-membrane spanning protein tyrosine kinase activity
D0004743molecular_functionpyruvate kinase activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005791cellular_componentrough endoplasmic reticulum
D0006096biological_processglycolytic process
D0006417biological_processregulation of translation
D0016301molecular_functionkinase activity
D0016740molecular_functiontransferase activity
D0030955molecular_functionpotassium ion binding
D0046872molecular_functionmetal ion binding
D1903672biological_processpositive regulation of sprouting angiogenesis
D2000767biological_processpositive regulation of cytoplasmic translation
E0000166molecular_functionnucleotide binding
E0000287molecular_functionmagnesium ion binding
E0003729molecular_functionmRNA binding
E0003824molecular_functioncatalytic activity
E0004674molecular_functionprotein serine/threonine kinase activity
E0004713molecular_functionprotein tyrosine kinase activity
E0004715molecular_functionnon-membrane spanning protein tyrosine kinase activity
E0004743molecular_functionpyruvate kinase activity
E0005515molecular_functionprotein binding
E0005524molecular_functionATP binding
E0005634cellular_componentnucleus
E0005737cellular_componentcytoplasm
E0005791cellular_componentrough endoplasmic reticulum
E0006096biological_processglycolytic process
E0006417biological_processregulation of translation
E0016301molecular_functionkinase activity
E0016740molecular_functiontransferase activity
E0030955molecular_functionpotassium ion binding
E0046872molecular_functionmetal ion binding
E1903672biological_processpositive regulation of sprouting angiogenesis
E2000767biological_processpositive regulation of cytoplasmic translation
F0000166molecular_functionnucleotide binding
F0000287molecular_functionmagnesium ion binding
F0003729molecular_functionmRNA binding
F0003824molecular_functioncatalytic activity
F0004674molecular_functionprotein serine/threonine kinase activity
F0004713molecular_functionprotein tyrosine kinase activity
F0004715molecular_functionnon-membrane spanning protein tyrosine kinase activity
F0004743molecular_functionpyruvate kinase activity
F0005515molecular_functionprotein binding
F0005524molecular_functionATP binding
F0005634cellular_componentnucleus
F0005737cellular_componentcytoplasm
F0005791cellular_componentrough endoplasmic reticulum
F0006096biological_processglycolytic process
F0006417biological_processregulation of translation
F0016301molecular_functionkinase activity
F0016740molecular_functiontransferase activity
F0030955molecular_functionpotassium ion binding
F0046872molecular_functionmetal ion binding
F1903672biological_processpositive regulation of sprouting angiogenesis
F2000767biological_processpositive regulation of cytoplasmic translation
G0000166molecular_functionnucleotide binding
G0000287molecular_functionmagnesium ion binding
G0003729molecular_functionmRNA binding
G0003824molecular_functioncatalytic activity
G0004674molecular_functionprotein serine/threonine kinase activity
G0004713molecular_functionprotein tyrosine kinase activity
G0004715molecular_functionnon-membrane spanning protein tyrosine kinase activity
G0004743molecular_functionpyruvate kinase activity
G0005515molecular_functionprotein binding
G0005524molecular_functionATP binding
G0005634cellular_componentnucleus
G0005737cellular_componentcytoplasm
G0005791cellular_componentrough endoplasmic reticulum
G0006096biological_processglycolytic process
G0006417biological_processregulation of translation
G0016301molecular_functionkinase activity
G0016740molecular_functiontransferase activity
G0030955molecular_functionpotassium ion binding
G0046872molecular_functionmetal ion binding
G1903672biological_processpositive regulation of sprouting angiogenesis
G2000767biological_processpositive regulation of cytoplasmic translation
H0000166molecular_functionnucleotide binding
H0000287molecular_functionmagnesium ion binding
H0003729molecular_functionmRNA binding
H0003824molecular_functioncatalytic activity
H0004674molecular_functionprotein serine/threonine kinase activity
H0004713molecular_functionprotein tyrosine kinase activity
H0004715molecular_functionnon-membrane spanning protein tyrosine kinase activity
H0004743molecular_functionpyruvate kinase activity
H0005515molecular_functionprotein binding
H0005524molecular_functionATP binding
H0005634cellular_componentnucleus
H0005737cellular_componentcytoplasm
H0005791cellular_componentrough endoplasmic reticulum
H0006096biological_processglycolytic process
H0006417biological_processregulation of translation
H0016301molecular_functionkinase activity
H0016740molecular_functiontransferase activity
H0030955molecular_functionpotassium ion binding
H0046872molecular_functionmetal ion binding
H1903672biological_processpositive regulation of sprouting angiogenesis
H2000767biological_processpositive regulation of cytoplasmic translation
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 Residues1792
DetailsRegion: {"description":"Interaction with POU5F1","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues200
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues40
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P30613","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P00549","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues15
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues16
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues24
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues16
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues16
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P11980","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues16
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues8
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues16
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues8
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues8
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues8
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues8
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues24
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues8
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues16
DetailsModified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 326
ChainResidueDetails
AARG72attractive charge-charge interaction, electrostatic stabiliser, steric role
AARG119attractive charge-charge interaction, electrostatic stabiliser, steric role
ALYS269attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role
ATHR327electrostatic stabiliser, hydrogen bond donor, increase acidity

site_idMCSA2
Number of Residues4
DetailsM-CSA 326
ChainResidueDetails
BARG72attractive charge-charge interaction, electrostatic stabiliser, steric role
BARG119attractive charge-charge interaction, electrostatic stabiliser, steric role
BLYS269attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role
BTHR327electrostatic stabiliser, hydrogen bond donor, increase acidity

site_idMCSA3
Number of Residues4
DetailsM-CSA 326
ChainResidueDetails
CARG72attractive charge-charge interaction, electrostatic stabiliser, steric role
CARG119attractive charge-charge interaction, electrostatic stabiliser, steric role
CLYS269attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role
CTHR327electrostatic stabiliser, hydrogen bond donor, increase acidity

site_idMCSA4
Number of Residues4
DetailsM-CSA 326
ChainResidueDetails
DARG72attractive charge-charge interaction, electrostatic stabiliser, steric role
DARG119attractive charge-charge interaction, electrostatic stabiliser, steric role
DLYS269attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role
DTHR327electrostatic stabiliser, hydrogen bond donor, increase acidity

site_idMCSA5
Number of Residues4
DetailsM-CSA 326
ChainResidueDetails
EARG72attractive charge-charge interaction, electrostatic stabiliser, steric role
EARG119attractive charge-charge interaction, electrostatic stabiliser, steric role
ELYS269attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role
ETHR327electrostatic stabiliser, hydrogen bond donor, increase acidity

site_idMCSA6
Number of Residues4
DetailsM-CSA 326
ChainResidueDetails
FARG72attractive charge-charge interaction, electrostatic stabiliser, steric role
FARG119attractive charge-charge interaction, electrostatic stabiliser, steric role
FLYS269attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role
FTHR327electrostatic stabiliser, hydrogen bond donor, increase acidity

site_idMCSA7
Number of Residues4
DetailsM-CSA 326
ChainResidueDetails
GARG72attractive charge-charge interaction, electrostatic stabiliser, steric role
GARG119attractive charge-charge interaction, electrostatic stabiliser, steric role
GLYS269attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role
GTHR327electrostatic stabiliser, hydrogen bond donor, increase acidity

site_idMCSA8
Number of Residues4
DetailsM-CSA 326
ChainResidueDetails
HARG72attractive charge-charge interaction, electrostatic stabiliser, steric role
HARG119attractive charge-charge interaction, electrostatic stabiliser, steric role
HLYS269attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role
HTHR327electrostatic stabiliser, hydrogen bond donor, increase acidity

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