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1KAG

Crystal Structure of the Escherichia coli Shikimate Kinase I (AroK)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0004765molecular_functionshikimate kinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008652biological_processamino acid biosynthetic process
A0009073biological_processaromatic amino acid family biosynthetic process
A0009423biological_processchorismate biosynthetic process
A0016301molecular_functionkinase activity
A0016740molecular_functiontransferase activity
A0019752biological_processcarboxylic acid metabolic process
A0046677biological_processresponse to antibiotic
A0046872molecular_functionmetal ion binding
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0004765molecular_functionshikimate kinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008652biological_processamino acid biosynthetic process
B0009073biological_processaromatic amino acid family biosynthetic process
B0009423biological_processchorismate biosynthetic process
B0016301molecular_functionkinase activity
B0016740molecular_functiontransferase activity
B0019752biological_processcarboxylic acid metabolic process
B0046677biological_processresponse to antibiotic
B0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS01128
Number of Residues26
DetailsSHIKIMATE_KINASE Shikimate kinase signature. RdrEekvIneltekqgi...VLAtGGGsV
ChainResidueDetails
AARG60-VAL85

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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