5V2M
Mevalonate diphosphate mediated ATP binding mechanism of the mevalonate diphosphate decarboxylase from Enterococcus faecalis
Summary for 5V2M
Entry DOI | 10.2210/pdb5v2m/pdb |
Related | 5V2L |
Descriptor | Mevalonate diphosphate decarboxylase, SULFATE ION (3 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 | 36798.63 |
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: 29025876DOI: 10.1074/jbc.M117.802223 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.989 Å) |
Structure validation
Download full validation report