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4A3S

Crystal structure of PFK from Bacillus subtilis

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0003872molecular_function6-phosphofructokinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005945cellular_component6-phosphofructokinase complex
A0006002biological_processfructose 6-phosphate metabolic process
A0006096biological_processglycolytic process
A0008443molecular_functionphosphofructokinase activity
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0030388biological_processfructose 1,6-bisphosphate metabolic process
A0046835biological_processcarbohydrate phosphorylation
A0046872molecular_functionmetal ion binding
A0061621biological_processcanonical glycolysis
A0070095molecular_functionfructose-6-phosphate binding
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0003872molecular_function6-phosphofructokinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005945cellular_component6-phosphofructokinase complex
B0006002biological_processfructose 6-phosphate metabolic process
B0006096biological_processglycolytic process
B0008443molecular_functionphosphofructokinase activity
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0030388biological_processfructose 1,6-bisphosphate metabolic process
B0046835biological_processcarbohydrate phosphorylation
B0046872molecular_functionmetal ion binding
B0061621biological_processcanonical glycolysis
B0070095molecular_functionfructose-6-phosphate binding
Functional Information from PROSITE/UniProt
site_idPS00433
Number of Residues19
DetailsPHOSPHOFRUCTOKINASE Phosphofructokinase signature. RvsvlGHiQRGGspsaaDR
ChainResidueDetails
AARG243-ARG261

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00339
ChainResidueDetails
AASP127
BASP127

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00339
ChainResidueDetails
AGLY11
BARG72
BGLY102
BASP103
BARG162
BARG243
AARG21
AARG72
AGLY102
AASP103
AARG162
AARG243
BGLY11
BARG21

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_00339
ChainResidueDetails
ATHR125
BARG154
BMET169
BGLY185
BARG211
BLYS213
BGLU222
BHIS249
AARG154
AMET169
AGLY185
AARG211
ALYS213
AGLU222
AHIS249
BTHR125

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PDB entries from 2025-06-18

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