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PDBe Entry: 1qay 
TERNARY COMPLEX OF PSEUDOMONAS MEVALONII HMG-COA REDUCTASE WITH MEVALONATE AND NAD+
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OXIDOREDUCTASE
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X-RAY DIFFRACTION
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Resolution: 2.8 Å, R-factor: 18.8%, Free R-factor: 26.6%, Spacegroup: I 41 3 2
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18/06/1999, deposition: 07/04/1999, last revision: 24/02/2009
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Tabernero, L.; Bochar, D.A.; Rodwell, V.W.; Stauffacher, C.V.
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Substrate-induced closure of the flap domain in the ternary complex structures provides insights into the mechanism of catalysis by 3-hydroxy-3-methylglutaryl-CoA reductase.
PROC.NATL.ACAD.SCI.USA vol:96, pag:7167-7171 (1999) [PubMed ID 10377386 ]
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4-ELECTRON OXIDO-REDUCTASE, OXIDOREDUCTASE
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1.1.1.88 ExPASy BRENDA (A B)
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Pseudomonas mevalonii 32044(A B)
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3-hydroxy-3-methylglutaryl-coenzyme A reductase (EC 1.1.1.88) (HMG-CoA reductase) P13702 (A B)
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A, B
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| A, B |
PROTEIN (3-HYDROXY-3-METHYLGLUTARYL-COENZYME A REDUCTASE) |
Protein |
P13702 (MVAA_PSEMV)
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428 |
89% |
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| B |
NICOTINAMIDE-ADENINE-DINUCLEOTIDE |
NAD
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| A |
(R)-MEVALONATE |
MEV
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