8QZJ

Crystal structure of PptT-ADP from Mycobacterium tuberculosis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0005515	molecular_function	protein binding
A	0005886	cellular_component	plasma membrane
A	0008897	molecular_function	holo-[acyl-carrier-protein] synthase activity
A	0009237	biological_process	siderophore metabolic process
A	0009239	biological_process	enterobactin biosynthetic process
A	0009366	cellular_component	enterobactin synthetase complex
A	0016740	molecular_function	transferase activity
A	0016780	molecular_function	phosphotransferase activity, for other substituted phosphate groups
A	0019290	biological_process	siderophore biosynthetic process
A	0046872	molecular_function	metal ion binding
B	0000287	molecular_function	magnesium ion binding
B	0005515	molecular_function	protein binding
B	0005886	cellular_component	plasma membrane
B	0008897	molecular_function	holo-[acyl-carrier-protein] synthase activity
B	0009237	biological_process	siderophore metabolic process
B	0009239	biological_process	enterobactin biosynthetic process
B	0009366	cellular_component	enterobactin synthetase complex
B	0016740	molecular_function	transferase activity
B	0016780	molecular_function	phosphotransferase activity, for other substituted phosphate groups
B	0019290	biological_process	siderophore biosynthetic process
B	0046872	molecular_function	metal ion binding
C	0000287	molecular_function	magnesium ion binding
C	0005515	molecular_function	protein binding
C	0005886	cellular_component	plasma membrane
C	0008897	molecular_function	holo-[acyl-carrier-protein] synthase activity
C	0009237	biological_process	siderophore metabolic process
C	0009239	biological_process	enterobactin biosynthetic process
C	0009366	cellular_component	enterobactin synthetase complex
C	0016740	molecular_function	transferase activity
C	0016780	molecular_function	phosphotransferase activity, for other substituted phosphate groups
C	0019290	biological_process	siderophore biosynthetic process
C	0046872	molecular_function	metal ion binding
D	0000287	molecular_function	magnesium ion binding
D	0005515	molecular_function	protein binding
D	0005886	cellular_component	plasma membrane
D	0008897	molecular_function	holo-[acyl-carrier-protein] synthase activity
D	0009237	biological_process	siderophore metabolic process
D	0009239	biological_process	enterobactin biosynthetic process
D	0009366	cellular_component	enterobactin synthetase complex
D	0016740	molecular_function	transferase activity
D	0016780	molecular_function	phosphotransferase activity, for other substituted phosphate groups
D	0019290	biological_process	siderophore biosynthetic process
D	0046872	molecular_function	metal ion binding

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	32
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24963544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25450595","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"AUG-2014","submissionDatabase":"PDB data bank","title":"X-ray structure of the 4'-phosphopantetheinyl transferase PptT from Mycobacterium tuberculosis.","authors":["Faille A.","Gavalda S.","Rottier K.","Mourey L.","Pedelacq J.D."]}}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"25450595","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4QVH","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24963544","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"AUG-2014","submissionDatabase":"PDB data bank","title":"X-ray structure of the 4'-phosphopantetheinyl transferase PptT from Mycobacterium tuberculosis.","authors":["Faille A.","Gavalda S.","Rottier K.","Mourey L.","Pedelacq J.D."]}}]}

Chain

Residue

Details

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