5V2L

Mevalonate diphosphate mediated ATP binding mechanism of the mevalonate diphosphate decarboxylase from Enterococcus faecalis

Summary for 5V2L

Entry DOI	10.2210/pdb5v2l/pdb
Related	5V2M
Descriptor	Mevalonate diphosphate decarboxylase, ADENOSINE-5'-TRIPHOSPHATE, PHOSPHATE ION, ... (4 entities in total)
Functional Keywords	the mevalonate pathway, vancomycin resistant enterococci, enzyme kinetics, isothermal titration calorimetry., lyase
Biological source	Enterococcus faecalis V583
Total number of polymer chains	1
Total formula weight	37304.71
Authors	Stauffacher, C.V.,Chen, C.-L. (deposition date: 2017-03-05, release date: 2017-10-18, Last modification date: 2023-10-04)
Primary citation	Chen, C.L.,Mermoud, J.C.,Paul, L.N.,Steussy, C.N.,Stauffacher, C.V. Mevalonate 5-diphosphate mediates ATP binding to the mevalonate diphosphate decarboxylase from the bacterial pathogen Enterococcus faecalis. J. Biol. Chem., 292:21340-21351, 2017 Cited by PubMed: 29025876 DOI: 10.1074/jbc.M117.802223 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.1 Å)

Structure validation