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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8F6M

Complex of Rabbit muscle pyruvate kinase with ADP and the phosphonate analogue of PEP mimicking the Michaelis complex.

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 Residues14
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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