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7S49

Crystal Structure of Inhibitor-bound Galactokinase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0004335molecular_functiongalactokinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005534molecular_functiongalactose binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006012biological_processgalactose metabolic process
A0016020cellular_componentmembrane
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
A0019402biological_processgalactitol metabolic process
A0033499biological_processgalactose catabolic process via UDP-galactose, Leloir pathway
A0046835biological_processcarbohydrate phosphorylation
A0061623biological_processglycolytic process from galactose
A0070062cellular_componentextracellular exosome
B0000166molecular_functionnucleotide binding
B0004335molecular_functiongalactokinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005534molecular_functiongalactose binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006012biological_processgalactose metabolic process
B0016020cellular_componentmembrane
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
B0019402biological_processgalactitol metabolic process
B0033499biological_processgalactose catabolic process via UDP-galactose, Leloir pathway
B0046835biological_processcarbohydrate phosphorylation
B0061623biological_processglycolytic process from galactose
B0070062cellular_componentextracellular exosome
Functional Information from PROSITE/UniProt
site_idPS00106
Number of Residues12
DetailsGALACTOKINASE Galactokinase signature. GRvNLIGEHtDY
ChainResidueDetails
AGLY36-TYR47

site_idPS00627
Number of Residues12
DetailsGHMP_KINASES_ATP GHMP kinases putative ATP-binding domain. VPlGgGLSSSAS
ChainResidueDetails
AVAL133-SER144

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"Q9HHB6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P04385","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"Q9HHB6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

240971

PDB entries from 2025-08-27

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