3PXU
Crystal structure of phosphopantetheine adenylyltransferase from Burkholderia pseudomallei bound to dephospho-coenzyme A
Replaces: 3IKZFunctional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004595 | molecular_function | pantetheine-phosphate adenylyltransferase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0015937 | biological_process | coenzyme A biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016779 | molecular_function | nucleotidyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE COD A 201 |
| Chain | Residue |
| A | TYR6 |
| A | PHE69 |
| A | GLY71 |
| A | LEU72 |
| A | LEU73 |
| A | ARG87 |
| A | GLY88 |
| A | ARG90 |
| A | GLU98 |
| A | MET101 |
| A | PRO119 |
| A | GLY8 |
| A | TYR123 |
| A | ILE126 |
| A | GLU133 |
| A | LEU137 |
| A | HOH179 |
| A | HOH193 |
| A | HOH199 |
| A | HOH216 |
| A | HOH244 |
| A | THR9 |
| A | PHE10 |
| A | GLY16 |
| A | HIS17 |
| A | LEU20 |
| A | ALA36 |
| A | LYS41 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 202 |
| Chain | Residue |
| A | GLU18 |
| A | VAL57 |
| A | HIS60 |
| A | TYR61 |
| A | PHE146 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 203 |
| Chain | Residue |
| A | ASP37 |
| A | ARG39 |
| A | PHE45 |
| A | SER46 |
| A | LEU47 |
| A | ARG50 |
| A | HOH217 |
| A | HOH230 |
| A | HOH231 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 204 |
| Chain | Residue |
| A | ARG15 |
| A | PHE146 |
| A | PRO147 |
| A | HOH227 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 205 |
| Chain | Residue |
| A | ARG90 |
| A | GLN100 |
| A | SER127 |
| A | GLY128 |
| A | THR129 |
| A | HOH199 |
| A | HOH259 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21904046","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3PXU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21904046","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3PXU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21904046","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3K9W","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PXU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21904046","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
