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4XYK

Crystal structure of human phosphofructokinase-1 in complex with ADP, Northeast Structural Genomics Consortium Target HR9275

Functional Information from GO Data
ChainGOidnamespacecontents
A0003872molecular_function6-phosphofructokinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005945cellular_component6-phosphofructokinase complex
A0006002biological_processfructose 6-phosphate metabolic process
A0006096biological_processglycolytic process
A0016020cellular_componentmembrane
A0016208molecular_functionAMP binding
A0016301molecular_functionkinase activity
A0030388biological_processfructose 1,6-bisphosphate metabolic process
A0042802molecular_functionidentical protein binding
A0044877molecular_functionprotein-containing complex binding
A0045296molecular_functioncadherin binding
A0046872molecular_functionmetal ion binding
A0048029molecular_functionmonosaccharide binding
A0061621biological_processcanonical glycolysis
A0070062cellular_componentextracellular exosome
A0070095molecular_functionfructose-6-phosphate binding
A1990830biological_processcellular response to leukemia inhibitory factor
B0003872molecular_function6-phosphofructokinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005945cellular_component6-phosphofructokinase complex
B0006002biological_processfructose 6-phosphate metabolic process
B0006096biological_processglycolytic process
B0016020cellular_componentmembrane
B0016208molecular_functionAMP binding
B0016301molecular_functionkinase activity
B0030388biological_processfructose 1,6-bisphosphate metabolic process
B0042802molecular_functionidentical protein binding
B0044877molecular_functionprotein-containing complex binding
B0045296molecular_functioncadherin binding
B0046872molecular_functionmetal ion binding
B0048029molecular_functionmonosaccharide binding
B0061621biological_processcanonical glycolysis
B0070062cellular_componentextracellular exosome
B0070095molecular_functionfructose-6-phosphate binding
B1990830biological_processcellular response to leukemia inhibitory factor
C0003872molecular_function6-phosphofructokinase activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005945cellular_component6-phosphofructokinase complex
C0006002biological_processfructose 6-phosphate metabolic process
C0006096biological_processglycolytic process
C0016020cellular_componentmembrane
C0016208molecular_functionAMP binding
C0016301molecular_functionkinase activity
C0030388biological_processfructose 1,6-bisphosphate metabolic process
C0042802molecular_functionidentical protein binding
C0044877molecular_functionprotein-containing complex binding
C0045296molecular_functioncadherin binding
C0046872molecular_functionmetal ion binding
C0048029molecular_functionmonosaccharide binding
C0061621biological_processcanonical glycolysis
C0070062cellular_componentextracellular exosome
C0070095molecular_functionfructose-6-phosphate binding
C1990830biological_processcellular response to leukemia inhibitory factor
D0003872molecular_function6-phosphofructokinase activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0005945cellular_component6-phosphofructokinase complex
D0006002biological_processfructose 6-phosphate metabolic process
D0006096biological_processglycolytic process
D0016020cellular_componentmembrane
D0016208molecular_functionAMP binding
D0016301molecular_functionkinase activity
D0030388biological_processfructose 1,6-bisphosphate metabolic process
D0042802molecular_functionidentical protein binding
D0044877molecular_functionprotein-containing complex binding
D0045296molecular_functioncadherin binding
D0046872molecular_functionmetal ion binding
D0048029molecular_functionmonosaccharide binding
D0061621biological_processcanonical glycolysis
D0070062cellular_componentextracellular exosome
D0070095molecular_functionfructose-6-phosphate binding
D1990830biological_processcellular response to leukemia inhibitory factor
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue ADP A 801
ChainResidue
ASER32
ASER130
DGLN99
AGLY33
ATYR64
AARG97
ACYS98
AARG102
AGLY127
AASP128
AGLY129

site_idAC2
Number of Residues6
Detailsbinding site for residue PO4 A 802
ChainResidue
AGLY233
ALYS264
AARG430
AARG434
AGLY467
AGLY468

site_idAC3
Number of Residues6
Detailsbinding site for residue PO4 A 803
ChainResidue
AARG44
AARG48
AVAL82
ASER83
ASER84
AARG632

site_idAC4
Number of Residues4
Detailsbinding site for residue PO4 A 804
ChainResidue
AARG481
AHIS671
BARG576
BARG665

site_idAC5
Number of Residues13
Detailsbinding site for residue ADP B 801
ChainResidue
BGLY33
BGLY34
BTYR64
BARG97
BCYS98
BARG102
BGLY127
BASP128
BGLY129
BSER130
BGLY133
BSER173
BARG219

site_idAC6
Number of Residues4
Detailsbinding site for residue PO4 B 802
ChainResidue
BGLY233
BLYS264
BARG430
BARG434

site_idAC7
Number of Residues6
Detailsbinding site for residue PO4 B 803
ChainResidue
BARG44
BARG48
BSER83
BSER84
BGLY599
BARG632

site_idAC8
Number of Residues12
Detailsbinding site for residue ADP C 801
ChainResidue
CGLY33
CGLY34
CARG97
CCYS98
CPHE101
CARG102
CGLY126
CGLY127
CASP128
CGLY129
CSER130
CLEU136

site_idAC9
Number of Residues6
Detailsbinding site for residue PO4 C 802
ChainResidue
CGLY233
CLYS264
CARG430
CARG434
CGLY467
CGLY468

site_idAD1
Number of Residues5
Detailsbinding site for residue PO4 C 803
ChainResidue
CARG44
CARG48
CSER83
CSER84
CARG632

site_idAD2
Number of Residues3
Detailsbinding site for residue PO4 C 804
ChainResidue
CHIS671
CGLN674
DARG665

site_idAD3
Number of Residues5
Detailsbinding site for residue PO4 C 805
ChainResidue
CARG97
CARG219
CARG310
DARG210
DARG301

site_idAD4
Number of Residues3
Detailsbinding site for residue PO4 D 801
ChainResidue
CARG576
CARG665
DARG481

site_idAD5
Number of Residues13
Detailsbinding site for residue ADP D 802
ChainResidue
AGLN99
DSER32
DGLY33
DTYR64
DARG97
DCYS98
DARG102
DGLY127
DASP128
DGLY129
DSER130
DGLY133
DLEU136

site_idAD6
Number of Residues6
Detailsbinding site for residue PO4 D 803
ChainResidue
DARG430
DARG434
DGLY467
DGLY468
DGLY233
DLYS264

site_idAD7
Number of Residues6
Detailsbinding site for residue PO4 D 804
ChainResidue
DARG44
DARG48
DSER83
DSER84
DLYS567
DARG632

Functional Information from PROSITE/UniProt
site_idPS00433
Number of Residues19
DetailsPHOSPHOFRUCTOKINASE Phosphofructokinase signature. RvtilGHvQRGGtpsafDR
ChainResidueDetails
AARG301-ARG319
AARG665-ARG683

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03184
ChainResidueDetails
AASP175
BASP175
CASP175
DASP175

site_idSWS_FT_FI2
Number of Residues32
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03184
ChainResidueDetails
AGLY34
BARG97
BGLY127
BASP128
BARG210
BARG301
BARG576
BARG665
CGLY34
CARG97
CGLY127
AARG97
CASP128
CARG210
CARG301
CARG576
CARG665
DGLY34
DARG97
DGLY127
DASP128
DARG210
AGLY127
DARG301
DARG576
DARG665
AASP128
AARG210
AARG301
AARG576
AARG665
BGLY34

site_idSWS_FT_FI3
Number of Residues40
DetailsBINDING: in other chain => ECO:0000255|HAMAP-Rule:MF_03184
ChainResidueDetails
ASER173
AARG744
BSER173
BMET217
BGLU273
BHIS307
BARG481
BTHR538
BMET583
BGLU639
BHIS671
AMET217
BARG744
CSER173
CMET217
CGLU273
CHIS307
CARG481
CTHR538
CMET583
CGLU639
CHIS671
AGLU273
CARG744
DSER173
DMET217
DGLU273
DHIS307
DARG481
DTHR538
DMET583
DGLU639
DHIS671
AHIS307
DARG744
AARG481
ATHR538
AMET583
AGLU639
AHIS671

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:19413330
ChainResidueDetails
AMET1
BMET1
CMET1
DMET1

site_idSWS_FT_FI5
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER6
ASER21
BSER6
BSER21
CSER6
CSER21
DSER6
DSER21

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P47859
ChainResidueDetails
ASER12
BSER12
CSER12
DSER12

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P47860
ChainResidueDetails
ASER142
BSER142
CSER142
DSER142

site_idSWS_FT_FI8
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:33607258, ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER386
BSER386
CSER386
DSER386

site_idSWS_FT_FI9
Number of Residues12
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS395
DLYS395
DLYS486
DLYS688
ALYS486
ALYS688
BLYS395
BLYS486
BLYS688
CLYS395
CLYS486
CLYS688

site_idSWS_FT_FI10
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455
ChainResidueDetails
ATYR651
BTYR651
CTYR651
DTYR651

site_idSWS_FT_FI11
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231
ChainResidueDetails
ASER783
BSER783
CSER783
DSER783

site_idSWS_FT_FI12
Number of Residues4
DetailsCARBOHYD: O-linked (GlcNAc) serine => ECO:0000250
ChainResidueDetails
ASER540
BSER540
CSER540
DSER540

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PDB entries from 2024-07-31

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