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2HIG

Crystal Structure of Phosphofructokinase apoenzyme from Trypanosoma brucei.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0003872molecular_function6-phosphofructokinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006002biological_processfructose 6-phosphate metabolic process
A0006096biological_processglycolytic process
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0020015cellular_componentglycosome
A0042301molecular_functionphosphate ion binding
A0046872molecular_functionmetal ion binding
A0061615biological_processglycolytic process through fructose-6-phosphate
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0003872molecular_function6-phosphofructokinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006002biological_processfructose 6-phosphate metabolic process
B0006096biological_processglycolytic process
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0020015cellular_componentglycosome
B0042301molecular_functionphosphate ion binding
B0046872molecular_functionmetal ion binding
B0061615biological_processglycolytic process through fructose-6-phosphate
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 488
ChainResidue
AALA259
AVAL260
AALA262
AARG317
ASER318

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 488
ChainResidue
BSER318
BHOH532
BALA259
BVAL260
BALA262
BARG317

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_03186","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03186","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19084537","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03186","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19084537","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"Important for substrate specificity; cannot use PPi as phosphoryl donor","evidences":[{"source":"HAMAP-Rule","id":"MF_03186","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1pfk
ChainResidueDetails
AGLY107
AASP229
AARG274
AARG173
ATHR227

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1pfk
ChainResidueDetails
BGLY107
BASP229
BARG274
BARG173
BTHR227

site_idCSA3
Number of Residues5
DetailsAnnotated By Reference To The Literature 1pfk
ChainResidueDetails
ALYS226
AGLY107
AASP229
AARG173
ATHR227

site_idCSA4
Number of Residues5
DetailsAnnotated By Reference To The Literature 1pfk
ChainResidueDetails
BLYS226
BGLY107
BASP229
BARG173
BTHR227

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PDB entries from 2025-12-24

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