Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2AJ4

Crystal structure of Saccharomyces cerevisiae Galactokinase in complex with galactose and Mg:AMPPNP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000411biological_processpositive regulation of transcription by galactose
A0000435biological_processpositive regulation of transcription from RNA polymerase II promoter by galactose
A0004335molecular_functiongalactokinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005667cellular_componenttranscription regulator complex
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006012biological_processgalactose metabolic process
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
A0033499biological_processgalactose catabolic process via UDP-galactose, Leloir pathway
A0046835biological_processcarbohydrate phosphorylation
B0000166molecular_functionnucleotide binding
B0000411biological_processpositive regulation of transcription by galactose
B0000435biological_processpositive regulation of transcription from RNA polymerase II promoter by galactose
B0004335molecular_functiongalactokinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005667cellular_componenttranscription regulator complex
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006012biological_processgalactose metabolic process
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
B0033499biological_processgalactose catabolic process via UDP-galactose, Leloir pathway
B0046835biological_processcarbohydrate phosphorylation
Functional Information from PROSITE/UniProt
site_idPS00106
Number of Residues12
DetailsGALACTOKINASE Galactokinase signature. GRvNLIGEHiDY
ChainResidueDetails
AGLY52-TYR63

site_idPS00627
Number of Residues12
DetailsGHMP_KINASES_ATP GHMP kinases putative ATP-binding domain. VPtGsGLSSSAA
ChainResidueDetails
AVAL162-ALA173

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 Residues28
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16115868","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2AJ4","evidenceCode":"ECO:0007744"}]}
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":"19779198","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

PDB statisticsPDBj update infoContact PDBjnumon