1OD6
The Crystal Structure of Phosphopantetheine adenylyltransferase from Thermus Thermophilus in complex with 4'-phosphopantetheine
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 SO4 A 1162 |
| Chain | Residue |
| A | HIS104 |
| A | ARG107 |
| A | GLN108 |
| A | ALA121 |
| A | THR122 |
| A | HOH2124 |
| A | HOH2157 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1163 |
| Chain | Residue |
| A | SER128 |
| A | SER129 |
| A | HOH2021 |
| A | HOH2158 |
| A | HOH2159 |
| A | HOH2160 |
| A | HIS16 |
| A | ARG91 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1164 |
| Chain | Residue |
| A | GLN84 |
| A | TYR110 |
| A | HOH2115 |
| A | HOH2161 |
| A | HOH2162 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PNS A 1161 |
| Chain | Residue |
| A | PRO6 |
| A | GLY7 |
| A | SER8 |
| A | LEU35 |
| A | GLY72 |
| A | LEU73 |
| A | LEU74 |
| A | ASN106 |
| A | MET131 |
| A | GLU134 |
| A | HOH2133 |
| A | HOH2151 |
| A | HOH2152 |
| A | HOH2153 |
| A | HOH2154 |
| A | HOH2155 |
| A | HOH2156 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 11 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"14684898","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1OD6","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"HAMAP-Rule","id":"MF_00151","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"14684898","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1OD6","evidenceCode":"ECO:0007744"}]} |
| 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 |
