6JBC
Phosphotransferase related to CoA biosynthesis pathway
Summary for 6JBC
| Entry DOI | 10.2210/pdb6jbc/pdb |
| Descriptor | Pantoate kinase, TETRAETHYLENE GLYCOL, GLYCEROL, ... (8 entities in total) |
| Functional Keywords | coa biosynthesis, transferase |
| Biological source | Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)) |
| Total number of polymer chains | 1 |
| Total formula weight | 33666.45 |
| Authors | Kita, A.,Kishimoto, A.,Shimosaka, T.,Tomita, H.,Yokooji, Y.,Imanaka, T.,Atomi, H.,Miki, K. (deposition date: 2019-01-25, release date: 2020-01-29, Last modification date: 2023-11-22) |
| Primary citation | Kita, A.,Kishimoto, A.,Shimosaka, T.,Tomita, H.,Yokooji, Y.,Imanaka, T.,Atomi, H.,Miki, K. Crystal structure of pantoate kinase from Thermococcus kodakarensis. Proteins, 88:718-724, 2020 Cited by PubMed Abstract: The coenzyme A biosynthesis pathways in most archaea involve two unique enzymes, pantoate kinase and phosphopantothenate synthetase, to convert pantoate to 4'-phosphopantothenate. Here, we report the first crystal structure of pantoate kinase from the hyperthermophilic archaeon, Thermococcus kodakarensis and its complex with ATP and a magnesium ion. The electron density for the adenosine moiety of ATP was very weak, which most likely relates to its broad nucleotide specificity. Based on the structure of the active site that contains a glycerol molecule, the pantoate binding site and the roles of the highly conserved residues are suggested. PubMed: 31697438DOI: 10.1002/prot.25852 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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