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5V2M

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

Summary for 5V2M
Entry DOI10.2210/pdb5v2m/pdb
Related5V2L
DescriptorMevalonate diphosphate decarboxylase, SULFATE ION (3 entities in total)
Functional Keywordsthe mevalonate pathway, vancomycin resistant enterococci, enzyme kinetics, isothermal titration calorimetry., lyase
Biological sourceEnterococcus faecalis V583
Total number of polymer chains1
Total formula weight36798.63
Authors
Stauffacher, C.V.,Chen, C.-L. (deposition date: 2017-03-05, release date: 2017-10-18, Last modification date: 2023-10-04)
Primary citationChen, 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 (1.989 Å)
Structure validation

218500

건을2024-04-17부터공개중

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