7N8E
PptT PAP(CoA) 9056 complex
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 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
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 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"25450595","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4QVH","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
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 |