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PDBe Entry: 2r42 
The Biochemical and Structural Basis for feedback Inhibition of Mevalonate Kinase and Isoprenoid Metabolism
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TRANSFERASE
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X-RAY DIFFRACTION
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Resolution: 2.4 Å, R-factor: 23.5%, Free R-factor: 27.2%, Spacegroup: P 21 21 2
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24/06/2008, deposition: 30/08/2007, last revision: 24/02/2009
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Fu, Z. ; Voynova, N.E. ; Miziorko, H.M. ; Kim, J.P.
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Biochemical and Structural Basis for Feedback Inhibition of Mevalonate Kinase and Isoprenoid Metabolism. BIOCHEMISTRY vol:47, pag:3715-3724 (2008) [PubMed ID 18302342 ]
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Mevalonate Kinase , Farnesyl Thiodiphosphate , ATP-binding , Cholesterol biosynthesis , Cytoplasm , Lipid synthesis , Nucleotide-binding , Peroxisome , Steroid biosynthesis , Sterol biosynthesis , Transferase
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2.7.1.36 ExPASy BRENDA (A)
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Rattus norvegicus(Norway rat) 10116 (A)
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Mevalonate kinase (EC 2.7.1.36) (MK) P17256 (A)
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A
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2r3v
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| A |
Mevalonate kinase |
Protein |
P17256 (KIME_RAT)
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395 |
96% |
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| A |
MAGNESIUM ION |
MG
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| A |
S-[(2E,6E)-3,7,11-TRIMETHYLDODECA-2,6,10-TRIENYL] TRIHYDROGEN THIODIPHOSPHATE |
FPS
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