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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

6PFK

PHOSPHOFRUCTOKINASE, INHIBITED T-STATE

Replaces:  5PFK
Functional Information from GO Data
ChainGOidnamespacecontents
A0003872molecular_function6-phosphofructokinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005945cellular_component6-phosphofructokinase complex
A0006002biological_processfructose 6-phosphate metabolic process
A0006096biological_processglycolytic process
A0008443molecular_functionphosphofructokinase activity
A0016208molecular_functionAMP binding
A0030388biological_processfructose 1,6-bisphosphate metabolic process
A0042802molecular_functionidentical protein binding
A0048029molecular_functionmonosaccharide binding
A0061621biological_processcanonical glycolysis
A0070095molecular_functionfructose-6-phosphate binding
B0003872molecular_function6-phosphofructokinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005945cellular_component6-phosphofructokinase complex
B0006002biological_processfructose 6-phosphate metabolic process
B0006096biological_processglycolytic process
B0008443molecular_functionphosphofructokinase activity
B0016208molecular_functionAMP binding
B0030388biological_processfructose 1,6-bisphosphate metabolic process
B0042802molecular_functionidentical protein binding
B0048029molecular_functionmonosaccharide binding
B0061621biological_processcanonical glycolysis
B0070095molecular_functionfructose-6-phosphate binding
C0003872molecular_function6-phosphofructokinase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005945cellular_component6-phosphofructokinase complex
C0006002biological_processfructose 6-phosphate metabolic process
C0006096biological_processglycolytic process
C0008443molecular_functionphosphofructokinase activity
C0016208molecular_functionAMP binding
C0030388biological_processfructose 1,6-bisphosphate metabolic process
C0042802molecular_functionidentical protein binding
C0048029molecular_functionmonosaccharide binding
C0061621biological_processcanonical glycolysis
C0070095molecular_functionfructose-6-phosphate binding
D0003872molecular_function6-phosphofructokinase activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005945cellular_component6-phosphofructokinase complex
D0006002biological_processfructose 6-phosphate metabolic process
D0006096biological_processglycolytic process
D0008443molecular_functionphosphofructokinase activity
D0016208molecular_functionAMP binding
D0030388biological_processfructose 1,6-bisphosphate metabolic process
D0042802molecular_functionidentical protein binding
D0048029molecular_functionmonosaccharide binding
D0061621biological_processcanonical glycolysis
D0070095molecular_functionfructose-6-phosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PGA A 325
ChainResidue
AARG154
BHOH338
AARG211
ALYS213
ALYS214
AHOH372
BARG21
BARG25
BGLY58
BASP59
site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PGA B 325
ChainResidue
AARG21
AARG25
AGLY58
AASP59
AHOH333
BARG154
BARG211
BLYS213
BLYS214
BHOH328
site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PGA C 325
ChainResidue
CARG154
CARG211
CLYS213
CLYS214
CHOH372
DARG21
DARG25
DGLY58
DASP59
DHOH347
site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PGA D 325
ChainResidue
CARG21
CARG25
CGLY55
CGLY58
CASP59
DARG154
DARG211
DLYS213
DLYS214
DHOH331
DHOH335
Functional Information from PROSITE/UniProt
site_idPS00433
Number of Residues19
DetailsPHOSPHOFRUCTOKINASE Phosphofructokinase signature. RvtvlGHvQRGGsptafDR
ChainResidueDetails
AARG243-ARG261
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00339","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00339","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues32
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00339","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"6115424","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues32
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_00339","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12390023","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6115424","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues24
DetailsBinding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_00339","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"6115424","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00339","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12390023","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6115424","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1pfk
ChainResidueDetails
AGLY11
AASP127
ATHR125
AARG72
AARG171
site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1pfk
ChainResidueDetails
BGLY11
BASP127
BTHR125
BARG72
BARG171
site_idCSA3
Number of Residues5
DetailsAnnotated By Reference To The Literature 1pfk
ChainResidueDetails
CGLY11
CASP127
CTHR125
CARG72
CARG171
site_idCSA4
Number of Residues5
DetailsAnnotated By Reference To The Literature 1pfk
ChainResidueDetails
DGLY11
DASP127
DTHR125
DARG72
DARG171

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PDB entries from 2026-04-01

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