Summary for 6V2L
| Entry DOI | 10.2210/pdb6v2l/pdb |
| Descriptor | Phosphoenolpyruvate carboxykinase (ATP), ADENOSINE-5'-TRIPHOSPHATE, ACETATE ION, ... (5 entities in total) |
| Functional Keywords | lyase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 60415.37 |
| Authors | Sokaribo, A.S.,Goldie, H.,Sanders, D. (deposition date: 2019-11-25, release date: 2019-12-11, Last modification date: 2023-10-11) |
| Primary citation | Sokaribo, A.,Novakovski, B.A.A.,Cotelesage, J.,White, A.P.,Sanders, D.,Goldie, H. Kinetic and structural analysis of Escherichia coli phosphoenolpyruvate carboxykinase mutants. Biochim Biophys Acta Gen Subj, 1864:129517-129517, 2020 Cited by PubMed Abstract: Phosphoenolpyruvate carboxykinase (PEPCK) is a metabolic enzyme in the gluconeogenesis pathway, where it catalyzes the reversible conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) and CO. The substrates for Escherichia coli PEPCK are OAA and MgATP, with Mn acting as a cofactor. Analysis of PEPCK structures have revealed amino acid residues involved in substrate/cofactor coordination during catalysis. PubMed: 31911238DOI: 10.1016/j.bbagen.2020.129517 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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