1.1.1.B52: 3-quinuclidinone reductase (NADH)
This is an abbreviated version!
For detailed information about 3-quinuclidinone reductase (NADH), go to the full flat file.
Word Map on EC 1.1.1.B52
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1.1.1.B52
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rhodotorula
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synthesis
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rubra
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pharmacology
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tumefaciens
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agrobacterium
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peg
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nicotinamide
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phosphate-dependent
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protomer
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nadh-dependent
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vapour-diffusion
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sitting-drop
- 1.1.1.B52
-
rhodotorula
- synthesis
- rubra
- pharmacology
- tumefaciens
-
agrobacterium
- peg
- nicotinamide
-
phosphate-dependent
-
protomer
-
nadh-dependent
-
vapour-diffusion
-
sitting-drop
Reaction
Synonyms
3-quinuclidinone reductase, alcohol dehydrogenase, ArQR, AtQR, BacC, NADHdependent 3-quinuclidionone reductase, QNR
ECTree
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Crystallization
Crystallization on EC 1.1.1.B52 - 3-quinuclidinone reductase (NADH)
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crystallized under a reservoir solution condition of 0.2 M ammonium acetate, 0.1 M HEPES pH 8.5 and 24% (w/v) PEG3350
purified recombinant His-tagged enzyme, enzyme AtQR and 2 mM NADH are crystallized from a reservoir solution containing of 0.2 M ammonium acetate, 0.1 M HEPES, pH 8.5, and 24% w/v PEG 3350, X-ray diffraction structure determination and analysis at 1.72 A resolution. Three NADH-bound protomers and one NADH-free protomer form a tetrameric structure in an asymmetric unit of crystals. NADH not only acts as a proton donor, but also contributes to the stability of the alpha7 helix. Molecular replacement using structure of meso-2,3-butanediol dehydrogenase, PDB ID 1GEG, from Klebsiella pneumoniae as template
sitting-drop vapour-diffusion method at 20°C. Crystals are obtained using a reservoir solution containing PEG 3350 as a precipitant. X-ray diffraction data are collected to 1.72 A resolution. The crystal belongs to space group P2(1), with unit-cell parameters a = 62.0, b = 126.4, c = 62.0 A, beta = 110.5, and is suggested to contain four molecules in the asymmetric unit