1O6B
Crystal structure of phosphopantetheine adenylyltransferase with ADP
Functional 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 | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 A 170 |
| Chain | Residue |
| A | HIS18 |
| A | ARG91 |
| A | SER128 |
| A | SER129 |
| A | ADP173 |
| A | HOH226 |
| A | HOH284 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 171 |
| Chain | Residue |
| A | HOH174 |
| A | HOH174 |
| A | HOH218 |
| A | HOH218 |
| A | ASP139 |
| A | ASP139 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 172 |
| Chain | Residue |
| A | SER3 |
| A | SER3 |
| A | LYS84 |
| A | LYS84 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ADP A 173 |
| Chain | Residue |
| A | GLY9 |
| A | SER10 |
| A | PHE11 |
| A | GLY17 |
| A | HIS18 |
| A | ILE21 |
| A | ARG88 |
| A | GLY89 |
| A | ARG91 |
| A | ALA120 |
| A | TYR124 |
| A | LEU127 |
| A | PO4170 |
| A | HOH243 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16021622","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1O6B","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16021622","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1O6B","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16021622","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
