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1K6M

Crystal Structure of Human Liver 6-Phosphofructo-2-Kinase/Fructose-2,6-Bisphosphatase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003824molecular_functioncatalytic activity
A0003873molecular_function6-phosphofructo-2-kinase activity
A0004331molecular_functionfructose-2,6-bisphosphate 2-phosphatase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0006000biological_processfructose metabolic process
A0006003biological_processfructose 2,6-bisphosphate metabolic process
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0008152biological_processmetabolic process
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
A0016740molecular_functiontransferase activity
A0016787molecular_functionhydrolase activity
A0019900molecular_functionkinase binding
A0031100biological_processanimal organ regeneration
A0032868biological_processresponse to insulin
A0033762biological_processresponse to glucagon
A0042594biological_processresponse to starvation
A0042802molecular_functionidentical protein binding
A0043540cellular_component6-phosphofructo-2-kinase/fructose-2,6-biphosphatase complex
A0046835biological_processcarbohydrate phosphorylation
A0051384biological_processresponse to glucocorticoid
A0051591biological_processresponse to cAMP
A0070095molecular_functionfructose-6-phosphate binding
A1904539biological_processnegative regulation of glycolytic process through fructose-6-phosphate
B0000166molecular_functionnucleotide binding
B0003824molecular_functioncatalytic activity
B0003873molecular_function6-phosphofructo-2-kinase activity
B0004331molecular_functionfructose-2,6-bisphosphate 2-phosphatase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0006000biological_processfructose metabolic process
B0006003biological_processfructose 2,6-bisphosphate metabolic process
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0008152biological_processmetabolic process
B0016301molecular_functionkinase activity
B0016310biological_processphosphorylation
B0016740molecular_functiontransferase activity
B0016787molecular_functionhydrolase activity
B0019900molecular_functionkinase binding
B0031100biological_processanimal organ regeneration
B0032868biological_processresponse to insulin
B0033762biological_processresponse to glucagon
B0042594biological_processresponse to starvation
B0042802molecular_functionidentical protein binding
B0043540cellular_component6-phosphofructo-2-kinase/fructose-2,6-biphosphatase complex
B0046835biological_processcarbohydrate phosphorylation
B0051384biological_processresponse to glucocorticoid
B0051591biological_processresponse to cAMP
B0070095molecular_functionfructose-6-phosphate binding
B1904539biological_processnegative regulation of glycolytic process through fructose-6-phosphate
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 501
ChainResidue
AARG257
AHIS258
AASN264
AARG307
AGLU327
AHIS392
AGLN393
AHOH742

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 A 502
ChainResidue
AARG352
ALYS356
ATYR367
AGLN393
AARG397
AHOH637
AHOH639
AHOH664
ATYR338

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE AGS A 503
ChainResidue
AALA51
AARG52
AGLY53
ALYS54
ATHR55
ATYR56
AASP130
ASER158
AASN169
AGLN172
AVAL173
ALYS174
AVAL222
AVAL248
ATYR429
AHOH603
AHOH658

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 B 501
ChainResidue
BARG257
BHIS258
BASN264
BARG307
BGLU327
BHIS392
BGLN393
BHOH613
BHOH636

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 B 502
ChainResidue
BTYR338
BARG352
BLYS356
BTYR367
BGLN393
BARG397
BHOH608
BHOH734

site_idAC6
Number of Residues19
DetailsBINDING SITE FOR RESIDUE AGS B 503
ChainResidue
BALA51
BARG52
BGLY53
BLYS54
BTHR55
BTYR56
BASP130
BSER158
BASN169
BGLN172
BVAL173
BLYS174
BVAL222
BTYR429
BHOH614
BHOH628
BHOH646
BHOH647
BHOH684

Functional Information from PROSITE/UniProt
site_idPS00175
Number of Residues10
DetailsPG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. LcRHGEsElN
ChainResidueDetails
ALEU255-ASN264

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000255
ChainResidueDetails
AASP130
ACYS160
BASP130
BCYS160

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Tele-phosphohistidine intermediate => ECO:0000250|UniProtKB:P07953
ChainResidueDetails
AHIS258
BHIS258

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000250|UniProtKB:P07953
ChainResidueDetails
AGLU327
BGLU327

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:12379646
ChainResidueDetails
AGLY48
AASN169
ATYR429
BGLY48
BASN169
BTYR429

site_idSWS_FT_FI5
Number of Residues20
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q16875
ChainResidueDetails
AARG81
AARG307
BARG81
BARG104
BTHR132
BARG138
BLYS174
BARG195
BTYR199
BARG257
BASN264
AARG104
BARG307
ATHR132
AARG138
ALYS174
AARG195
ATYR199
AARG257
AASN264

site_idSWS_FT_FI6
Number of Residues16
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P07953
ChainResidueDetails
AGLY270
BTYR338
BPHE349
BARG352
BLYS356
BTYR367
BGLN393
BARG397
ATYR338
APHE349
AARG352
ALYS356
ATYR367
AGLN393
AARG397
BGLY270

site_idSWS_FT_FI7
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000250|UniProtKB:P00950
ChainResidueDetails
AHIS392
BHIS392

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P07953
ChainResidueDetails
ASER140
BSER140

218853

PDB entries from 2024-04-24

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