4U89
4'-phosphopantetheinyl transferase PptT 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 | 34 |
| Details | binding site for residue COA A 301 |
| Chain | Residue |
| A | ARG48 |
| A | THR92 |
| A | HIS93 |
| A | ASP114 |
| A | ASN123 |
| A | GLY124 |
| A | LYS156 |
| A | GLU157 |
| A | TYR160 |
| A | LYS161 |
| A | PHE164 |
| A | PHE52 |
| A | TRP170 |
| A | LEU171 |
| A | GLY172 |
| A | PHE173 |
| A | HOH401 |
| A | HOH438 |
| A | HOH443 |
| A | HOH467 |
| A | HOH491 |
| A | HOH493 |
| A | ARG56 |
| A | HOH503 |
| A | HOH509 |
| A | HOH510 |
| A | HOH515 |
| A | HOH523 |
| A | LYS75 |
| A | LYS78 |
| A | GLY79 |
| A | GLU80 |
| A | PRO81 |
| A | LEU91 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 302 |
| Chain | Residue |
| A | ASP137 |
| A | THR141 |
| A | THR179 |
| A | PHE180 |
| A | HOH513 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue NA A 303 |
| Chain | Residue |
| A | HIS177 |
| A | THR179 |
| A | VAL192 |
| A | HOH431 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 304 |
| Chain | Residue |
| A | PRO72 |
| A | LEU74 |
| A | CYS82 |
| A | HOH540 |
| A | HOH616 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue NA A 305 |
| Chain | Residue |
| A | TYR25 |
| A | HOH543 |
| A | HOH650 |
| A | HOH666 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue NA A 306 |
| Chain | Residue |
| A | CYS94 |
| A | ALA95 |
| A | HOH486 |
| A | HOH487 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue NA A 307 |
| Chain | Residue |
| A | HOH417 |
| A | HOH534 |
| A | HOH556 |
| A | HOH571 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 308 |
| Chain | Residue |
| A | TRP83 |
| A | GLY89 |
| A | PRO165 |
| A | HOH500 |
| A | HOH507 |
| A | HOH663 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue NA A 309 |
| Chain | Residue |
| A | PRO143 |
| A | PG4314 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue NA A 310 |
| Chain | Residue |
| A | PRO35 |
| A | HOH403 |
| A | HOH456 |
| A | HOH484 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 311 |
| Chain | Residue |
| A | GLU17 |
| A | PRO33 |
| A | PRO35 |
| A | HOH435 |
| A | HOH444 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue NA A 312 |
| Chain | Residue |
| A | HOH419 |
| A | HOH519 |
| A | HOH539 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue PO4 A 313 |
| Chain | Residue |
| A | SER44 |
| A | ARG48 |
| A | HOH464 |
| A | HOH512 |
| A | HOH532 |
| A | HOH561 |
| A | HOH619 |
| site_id | AD5 |
| Number of Residues | 8 |
| Details | binding site for residue PG4 A 314 |
| Chain | Residue |
| A | ALA42 |
| A | ARG49 |
| A | ARG140 |
| A | MET142 |
| A | ASP183 |
| A | SER184 |
| A | GLY186 |
| A | NA309 |
| site_id | AD6 |
| Number of Residues | 1 |
| Details | binding site for residue IMD A 315 |
| Chain | Residue |
| A | TRP170 |
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 |
