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2HW1

Crystal structure of human ketohexokinase complexed to different sugar molecules

Functional Information from GO Data
ChainGOidnamespacecontents
A0004454molecular_functionketohexokinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006000biological_processfructose metabolic process
A0006796biological_processphosphate-containing compound metabolic process
A0009744biological_processresponse to sucrose
A0009749biological_processresponse to glucose
A0009750biological_processresponse to fructose
A0010043biological_processresponse to zinc ion
A0016301molecular_functionkinase activity
A0016310biological_processphosphorylation
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
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:19237742, ECO:0007744|PDB:2HW1
ChainResidueDetails
AASP15

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0007744|PDB:2HW1
ChainResidueDetails
AGLY41
AASN42
AASN45
AASP258

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000305|PubMed:19237742, ECO:0007744|PDB:2HW1
ChainResidueDetails
AARG108
AALA226
AGLY255

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1lio
ChainResidueDetails
AASP258
AARG108

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1lio
ChainResidueDetails
AGLY257
AGLY255
AASP258
AALA256

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PDB entries from 2024-09-11

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