5WPJ
Structure of the class II 3-hydroxy-3-methylglutaryl-CoA reductase from Streptococcus pneumoniae bound to NADPH in open conformations
Summary for 5WPJ
Entry DOI | 10.2210/pdb5wpj/pdb |
Descriptor | 3-hydroxy-3-methylglutaryl coenzyme A reductase, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, GLYCEROL, ... (4 entities in total) |
Functional Keywords | 3-hydroxy-3-methylglutaryl-coa reductase, hmg-coa, conformational change, oxidoreductase |
Biological source | Streptococcus pneumoniae |
Total number of polymer chains | 4 |
Total formula weight | 186945.08 |
Authors | Miller, B.R.,Kung, Y. (deposition date: 2017-08-04, release date: 2018-04-25, Last modification date: 2023-10-04) |
Primary citation | Miller, B.R.,Kung, Y. Structural Features and Domain Movements Controlling Substrate Binding and Cofactor Specificity in Class II HMG-CoA Reductase. Biochemistry, 57:654-662, 2018 Cited by PubMed: 29224355DOI: 10.1021/acs.biochem.7b00999 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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