6V2M

Structure of Escherichia coli Asp269Asn mutant phosphoenolpyruvate carboxykinase

Summary for 6V2M

Entry DOI	10.2210/pdb6v2m/pdb
Descriptor	Phosphoenolpyruvate carboxykinase (ATP), ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (5 entities in total)
Functional Keywords	lyase, enzyme, phosphoenolpyruvate carboxykinase
Biological source	Escherichia coli
Total number of polymer chains	1
Total formula weight	60356.89
Authors	Sokaribo, A.S.,Cotelesage, J.H. (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: 31911238 DOI: 10.1016/j.bbagen.2020.129517 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.66 Å)

Structure validation