3HR7

Crystal structure of the shikimate kinase-sulfate complex from Helicobacter pylori

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion binding
A	0004765	molecular_function	shikimate kinase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0008652	biological_process	amino acid biosynthetic process
A	0009073	biological_process	aromatic amino acid family biosynthetic process
A	0009423	biological_process	chorismate biosynthetic process
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0019752	biological_process	carboxylic acid metabolic process
A	0046872	molecular_function	metal ion binding
B	0000166	molecular_function	nucleotide binding
B	0000287	molecular_function	magnesium ion binding
B	0004765	molecular_function	shikimate kinase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0008652	biological_process	amino acid biosynthetic process
B	0009073	biological_process	aromatic amino acid family biosynthetic process
B	0009423	biological_process	chorismate biosynthetic process
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
B	0019752	biological_process	carboxylic acid metabolic process
B	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

Functional Information from PROSITE/UniProt

site_id	PS01128
Number of Residues	27
Details	SHIKIMATE_KINASE Shikimate kinase signature. RmfEknlIdelktlktph..VIStGGGiV

Chain	Residue	Details
A	ARG57-VAL83

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

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Chain

Residue

Details