7ED0
Transferase 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 32 |
| Details | binding site for residue COA A 301 |
| Chain | Residue |
| A | ARG48 |
| A | THR92 |
| A | HIS93 |
| A | ASP114 |
| A | ASN123 |
| A | LYS156 |
| A | GLU157 |
| A | TYR160 |
| A | LYS161 |
| A | PHE164 |
| A | TRP170 |
| A | PHE52 |
| A | LEU171 |
| A | GLY172 |
| A | PHE173 |
| A | HOH406 |
| A | HOH410 |
| A | HOH424 |
| A | HOH426 |
| A | HOH428 |
| A | HOH437 |
| A | HOH443 |
| A | ARG56 |
| A | HOH451 |
| A | HOH466 |
| A | HOH467 |
| A | LYS75 |
| A | LYS78 |
| A | GLY79 |
| A | GLU80 |
| A | PRO81 |
| A | LEU91 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 302 |
| Chain | Residue |
| A | SER44 |
| A | ARG48 |
| A | HOH409 |
| A | HOH441 |
| A | HOH452 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 303 |
| Chain | Residue |
| A | PRO12 |
| A | ARG190 |
| A | ARG211 |
| A | ARG213 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| 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 | 3 |
| 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 | 1 |
| 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 |
