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5WBZ

Structure of human Ketohexokinase complexed with hits from fragment screening

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004454molecular_functionketohexokinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006000biological_processfructose metabolic process
A0009744biological_processresponse to sucrose
A0009749biological_processresponse to glucose
A0009750biological_processresponse to fructose
A0010043biological_processresponse to zinc ion
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0032868biological_processresponse to insulin
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0046835biological_processcarbohydrate phosphorylation
A0070061molecular_functionfructose binding
A0070062cellular_componentextracellular exosome
A0070873biological_processregulation of glycogen metabolic process
B0000166molecular_functionnucleotide binding
B0004454molecular_functionketohexokinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006000biological_processfructose metabolic process
B0009744biological_processresponse to sucrose
B0009749biological_processresponse to glucose
B0009750biological_processresponse to fructose
B0010043biological_processresponse to zinc ion
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0032868biological_processresponse to insulin
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0046835biological_processcarbohydrate phosphorylation
B0070061molecular_functionfructose binding
B0070062cellular_componentextracellular exosome
B0070873biological_processregulation of glycogen metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues17
Detailsbinding site for residue A4J A 301
ChainResidue
AASN107
AALA285
AGLY286
ACYS289
AHOH402
AHOH412
AHOH436
BASP27
BHOH402
AALA224
AALA226
AGLU227
APRO246
APRO247
ATHR253
AGLY257
APHE260

site_idAC2
Number of Residues8
Detailsbinding site for residue SO4 A 302
ChainResidue
AARG108
ATHR253
AGLY255
AALA256
AGLY257
AASP258
AHOH456
BHOH435

site_idAC3
Number of Residues11
Detailsbinding site for residue CIT A 303
ChainResidue
ALEU11
AVAL13
AASP15
AGLY41
AASN42
ASER97
AILE110
AGLU139
ALYS174
AHOH403
BGLU29

site_idAC4
Number of Residues14
Detailsbinding site for residue A4J B 301
ChainResidue
BALA224
BALA226
BGLU227
BPRO246
BPRO247
BTHR253
BGLY257
BPHE260
BGLY286
BCYS289
BHOH408
BHOH418
BHOH420
BHOH424

site_idAC5
Number of Residues5
Detailsbinding site for residue SO4 B 302
ChainResidue
BARG78
BARG79
BGLY293
BPHE294
BHOH404

site_idAC6
Number of Residues4
Detailsbinding site for residue SO4 B 303
ChainResidue
AARG31
BHIS113
BARG141
BLYS174

site_idAC7
Number of Residues8
Detailsbinding site for residue CIT B 304
ChainResidue
AARG272
AGLU276
AHOH413
BPHE266
BSER267
BGLN270
BARG272
BPHE280

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19237742","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2HW1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PDB","id":"2HW1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19237742","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2HW1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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