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

3UQD

Crystal structure of the Phosphofructokinase-2 from Escherichia coli in complex with substrates and products

Functional Information from GO Data
ChainGOidnamespacecontents
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
A0009024molecular_functiontagatose-6-phosphate kinase activity
A0016301molecular_functionkinase activity
A0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
A0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
A0061615biological_processglycolytic process through fructose-6-phosphate
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
B0009024molecular_functiontagatose-6-phosphate kinase activity
B0016301molecular_functionkinase activity
B0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
B0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
B0061615biological_processglycolytic process through fructose-6-phosphate
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
C0009024molecular_functiontagatose-6-phosphate kinase activity
C0016301molecular_functionkinase activity
C0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
C0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
C0042802molecular_functionidentical protein binding
C0042803molecular_functionprotein homodimerization activity
C0046872molecular_functionmetal ion binding
C0061615biological_processglycolytic process through fructose-6-phosphate
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
D0009024molecular_functiontagatose-6-phosphate kinase activity
D0016301molecular_functionkinase activity
D0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
D0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
D0042802molecular_functionidentical protein binding
D0042803molecular_functionprotein homodimerization activity
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
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AASP256
BASP256
CASP256
DASP256

site_idSWS_FT_FI2
Number of Residues20
DetailsBINDING:
ChainResidueDetails
ASER12
BASP256
CSER12
CGLY39
CARG90
CSER139
CASP256
DSER12
DGLY39
DARG90
DSER139
AGLY39
DASP256
AARG90
ASER139
AASP256
BSER12
BGLY39
BARG90
BSER139

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:18762190, ECO:0007744|PDB:3CQD
ChainResidueDetails
ALYS27
BLYS27
CLYS27
DLYS27

site_idSWS_FT_FI4
Number of Residues20
DetailsBINDING: in other chain => ECO:0000269|PubMed:18762190, ECO:0000269|PubMed:23823238, ECO:0000269|Ref.10, ECO:0000269|Ref.11, ECO:0007744|PDB:3CQD
ChainResidueDetails
ALYS185
BSER284
CLYS185
CSER224
CSER248
CVAL280
CSER284
DLYS185
DSER224
DSER248
DVAL280
ASER224
DSER284
ASER248
AVAL280
ASER284
BLYS185
BSER224
BSER248
BVAL280

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: in other chain => ECO:0000269|PubMed:18762190, ECO:0007744|PDB:3CQD
ChainResidueDetails
AASN187
BASN187
CASN187
DASN187

site_idSWS_FT_FI6
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AGLU190
BGLU190
CGLU190
DGLU190

site_idSWS_FT_FI7
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:23823238
ChainResidueDetails
ASER250
BASN289
BGLY291
BARG293
CSER250
CVAL252
CALA286
CASN289
CGLY291
CARG293
DSER250
AVAL252
DVAL252
DALA286
DASN289
DGLY291
DARG293
AALA286
AASN289
AGLY291
AARG293
BSER250
BVAL252
BALA286

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon