DELTA4-3-oxosteroid 5beta-reductase

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Word Map on EC




3-oxo-DELTA4-steroid 5beta-reductase, 4,5beta-dihydrocortisone:NADP+ DELTA4-oxidoreductase, 5-beta-reductase, 5beta-POR, 5beta-red, AKR1D1, aldo-keto reductase, aldo-keto reductase 1D1, aldo–keto reductase 1D1, androstenedione 5beta-reductase, cortisone 5beta-reductase, cortisone beta-reductase, DELTA 4-5beta-reductase, DELTA4-3-ketosteroid 5beta-reductase, DELTA4-3-oxosteroid 5beta-reductase, DELTA4-hydrogenase, EC, h5beta-red, h5beta-reductase, More, P5betaR, progesterone 5beta-reductase, reductase, cholestenone 5beta.-, reductase, cortisone DELTA4-5beta-, steroid 5beta-reductase, steroid 5beta.-reductase, testosterone 5-beta-reductase, testosterone 5beta-reductase


     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.1 With NAD+ or NADP+ as acceptor
       DELTA4-3-oxosteroid 5beta-reductase


Crystallization on EC - DELTA4-3-oxosteroid 5beta-reductase

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5beta-POR, in the presence and absence of the cofactor NADP+, hanging drop vapour diffusion method, using 15% polyethylene glycol 4000, 0.1 M ammonium acetate, and 0.1 M sodium citrate, pH 5.6
by the hanging-drop method, at 2.7 A resolution, crystals belong to space group P43212, contain a single 5beta-POR molecule in the asymmetric unit and tend to diffract anisotropically, identification of six out of eight possible Se-atom positions
recombinant wild-type and mutant enzymes from Escherichia coli strain M15 by nickel affinity chromatography
the crystal structure of the 5beta-POR-NADP+ binary complex reveals that 5beta-POR exhibits a characteristic short-chain dehydrogenase fold with an N-terminal domain consisting of a double Rossmann fold for cofactor binding and an insertional domain between strands betaF and betaG of about 100 residues for substrate binding, crystal structure of the 5beta-POR-NADP+ binary complex reveals that the side chain of K147 is found in a similar position to the lysine residue of the YXX(S)K motif in standard short-chain dehydrogenases
enzyme in binary complex with product NADP+, containing two monomers of AKR1D1, each of which consists of a 325-residue polypeptide chain that adopts an (alpha/beta)8-barrel fold, the AKR1D1-NADP+ complex adopts an extended anti-conformation, X-ray diffraction structure determination and analysis at 1.79 A resolution, comparison with other enzyme binary and tertiary ligand complex structures, overview
hanging drop vapour diffusion method in 20% (w/v) PEG-4K, 0.1 M sodium cacodylate (pH 6.5), 0.2 M sodium citrate, 0.5 M (NH4)2SO4
hanging drop vapour diffusion method, in 0.1 M Tris/HEPES (pH 7.5), 10-20% (w/v) polyethylene glycol 4000, and 10% isopropyl alcohol
purifed recombinant h5beta-red in ternary complex with NADPH and androstenedione, hanging-drop vapor diffusion technique, 2:1 v/v ratio of protein and well solution, about 5 days, X-ray diffraction structure determination and analysis at 2.0-2.3 A resolution