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3QAI

X-ray Structure of ketohexokinase in complex with a pyrimidopyrimidine analog 3

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 Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 301
ChainResidue
AARG108
AGLY255
AALA256
AGLY257
AASP258

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE XNN A 302
ChainResidue
AGLY229
AALA230
APRO246
AVAL250
ATHR253
AALA256
AGLY257
APHE260
ACYS282
BASP27
AASN107
AALA224
AALA226
AGLU227

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 301
ChainResidue
AARG31
BHIS113
BARG141
BLYS174
BARG176

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 302
ChainResidue
BARG78
BARG79
BPHE294

site_idAC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE XNN B 303
ChainResidue
BALA224
BALA226
BGLU227
BGLY229
BPHE245
BPRO246
BPRO247
BVAL250
BTHR253
BGLY257
BCYS282
BALA285
BCYS289

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

242842

PDB entries from 2025-10-08

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