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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

3N1C

Crystal structure of the phosphofructokinase-2 from Escherichia coli in complex with fructose-6-phosphate

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0003872molecular_function6-phosphofructokinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0006096biological_processglycolytic process
A0006974biological_processDNA damage response
A0008443molecular_functionphosphofructokinase activity
A0009024molecular_functiontagatose-6-phosphate kinase activity
A0016052biological_processcarbohydrate catabolic process
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0044281biological_processsmall molecule metabolic process
A0046835biological_processcarbohydrate phosphorylation
A0046872molecular_functionmetal ion binding
A0061615biological_processglycolytic process through fructose-6-phosphate
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0003872molecular_function6-phosphofructokinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0006096biological_processglycolytic process
B0006974biological_processDNA damage response
B0008443molecular_functionphosphofructokinase activity
B0009024molecular_functiontagatose-6-phosphate kinase activity
B0016052biological_processcarbohydrate catabolic process
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0044281biological_processsmall molecule metabolic process
B0046835biological_processcarbohydrate phosphorylation
B0046872molecular_functionmetal ion binding
B0061615biological_processglycolytic process through fructose-6-phosphate
C0000166molecular_functionnucleotide binding
C0000287molecular_functionmagnesium ion binding
C0003872molecular_function6-phosphofructokinase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005829cellular_componentcytosol
C0005975biological_processcarbohydrate metabolic process
C0006096biological_processglycolytic process
C0006974biological_processDNA damage response
C0008443molecular_functionphosphofructokinase activity
C0009024molecular_functiontagatose-6-phosphate kinase activity
C0016052biological_processcarbohydrate catabolic process
C0016301molecular_functionkinase activity
C0016740molecular_functiontransferase activity
C0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
C0042802molecular_functionidentical protein binding
C0042803molecular_functionprotein homodimerization activity
C0044281biological_processsmall molecule metabolic process
C0046835biological_processcarbohydrate phosphorylation
C0046872molecular_functionmetal ion binding
C0061615biological_processglycolytic process through fructose-6-phosphate
D0000166molecular_functionnucleotide binding
D0000287molecular_functionmagnesium ion binding
D0003872molecular_function6-phosphofructokinase activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005829cellular_componentcytosol
D0005975biological_processcarbohydrate metabolic process
D0006096biological_processglycolytic process
D0006974biological_processDNA damage response
D0008443molecular_functionphosphofructokinase activity
D0009024molecular_functiontagatose-6-phosphate kinase activity
D0016052biological_processcarbohydrate catabolic process
D0016301molecular_functionkinase activity
D0016740molecular_functiontransferase activity
D0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
D0042802molecular_functionidentical protein binding
D0042803molecular_functionprotein homodimerization activity
D0044281biological_processsmall molecule metabolic process
D0046835biological_processcarbohydrate phosphorylation
D0046872molecular_functionmetal ion binding
D0061615biological_processglycolytic process through fructose-6-phosphate
Functional Information from PROSITE/UniProt
site_idPS00583
Number of Residues25
DetailsPFKB_KINASES_1 pfkB family of carbohydrate kinases signature 1. GGgGiNVAraIaHLGgsataifpaG
ChainResidueDetails
AGLY38-GLY62
site_idPS00584
Number of Residues14
DetailsPFKB_KINASES_2 pfkB family of carbohydrate kinases signature 2. STvGAGDsmvGAMT
ChainResidueDetails
ASER250-THR263
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues48
DetailsBinding site: {}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18762190","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3CQD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues40
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"18762190","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23823238","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2011","submissionDatabase":"PDB data bank","title":"Structure of E. coli PFK2 in complex with substrates and products.","authors":["Pereira H.M.","Caniuguir A.","Baez M.","Cabrera R.","Garratt R.C.","Babul J."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2011","submissionDatabase":"PDB data bank","title":"Structure of E. coli PFK2 mutant Y23D.","authors":["Pereira H.M.","Caniuguir A.","Baez M.","Cabrera R.","Garratt R.C.","Babul J."]}},{"source":"PDB","id":"3CQD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues8
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"PubMed","id":"18762190","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3CQD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues21
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"23823238","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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PDB entries from 2025-11-05

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