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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

4XZ2

Human platelet phosphofructokinase in an R-state in complex with ADP and F6P, crystal form I

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0003872molecular_function6-phosphofructokinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005945cellular_component6-phosphofructokinase complex
A0006002biological_processfructose 6-phosphate metabolic process
A0006096biological_processglycolytic process
A0016020cellular_componentmembrane
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0030388biological_processfructose 1,6-bisphosphate metabolic process
A0044877molecular_functionprotein-containing complex binding
A0045296molecular_functioncadherin binding
A0046872molecular_functionmetal ion binding
A0061621biological_processcanonical glycolysis
A0070062cellular_componentextracellular exosome
A0070095molecular_functionfructose-6-phosphate binding
A1990830biological_processcellular response to leukemia inhibitory factor
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0003872molecular_function6-phosphofructokinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005945cellular_component6-phosphofructokinase complex
B0006002biological_processfructose 6-phosphate metabolic process
B0006096biological_processglycolytic process
B0016020cellular_componentmembrane
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0030388biological_processfructose 1,6-bisphosphate metabolic process
B0044877molecular_functionprotein-containing complex binding
B0045296molecular_functioncadherin binding
B0046872molecular_functionmetal ion binding
B0061621biological_processcanonical glycolysis
B0070062cellular_componentextracellular exosome
B0070095molecular_functionfructose-6-phosphate binding
B1990830biological_processcellular response to leukemia inhibitory factor
C0000166molecular_functionnucleotide binding
C0003824molecular_functioncatalytic activity
C0003872molecular_function6-phosphofructokinase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005945cellular_component6-phosphofructokinase complex
C0006002biological_processfructose 6-phosphate metabolic process
C0006096biological_processglycolytic process
C0016020cellular_componentmembrane
C0016301molecular_functionkinase activity
C0016740molecular_functiontransferase activity
C0030388biological_processfructose 1,6-bisphosphate metabolic process
C0044877molecular_functionprotein-containing complex binding
C0045296molecular_functioncadherin binding
C0046872molecular_functionmetal ion binding
C0061621biological_processcanonical glycolysis
C0070062cellular_componentextracellular exosome
C0070095molecular_functionfructose-6-phosphate binding
C1990830biological_processcellular response to leukemia inhibitory factor
D0000166molecular_functionnucleotide binding
D0003824molecular_functioncatalytic activity
D0003872molecular_function6-phosphofructokinase activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0005945cellular_component6-phosphofructokinase complex
D0006002biological_processfructose 6-phosphate metabolic process
D0006096biological_processglycolytic process
D0016020cellular_componentmembrane
D0016301molecular_functionkinase activity
D0016740molecular_functiontransferase activity
D0030388biological_processfructose 1,6-bisphosphate metabolic process
D0044877molecular_functionprotein-containing complex binding
D0045296molecular_functioncadherin binding
D0046872molecular_functionmetal ion binding
D0061621biological_processcanonical glycolysis
D0070062cellular_componentextracellular exosome
D0070095molecular_functionfructose-6-phosphate binding
D1990830biological_processcellular response to leukemia inhibitory factor
Functional Information from PROSITE/UniProt
site_idPS00433
Number of Residues19
DetailsPHOSPHOFRUCTOKINASE Phosphofructokinase signature. RvtilGHvQRGGtpsafDR
ChainResidueDetails
AARG301-ARG319
AARG665-ARG683
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues44
DetailsRegion: {"description":"Interdomain linker"}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues38
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03184","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues76
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_03184","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P47860","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"33607258","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16964243","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues12
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues4
DetailsGlycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_03184","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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PDB entries from 2025-11-05

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