1.3.1.24: biliverdin reductase
This is an abbreviated version!
For detailed information about biliverdin reductase, go to the full flat file.
Word Map on EC 1.3.1.24
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1.3.1.24
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heme
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oxygenase-1
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monoxide
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cytoprotective
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repolarization
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beat-to-beat
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rosenthal
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hyperbilirubinemia
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palliation
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tetrapyrrole
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tdp
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torsades
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diagnostics
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proarrhythmia
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medicine
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galenic
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univentricular
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pharmacology
- 1.3.1.24
- heme
- oxygenase-1
-
monoxide
-
cytoprotective
-
repolarization
-
beat-to-beat
-
rosenthal
-
hyperbilirubinemia
-
palliation
- tetrapyrrole
- tdp
-
torsades
- diagnostics
-
proarrhythmia
- medicine
-
galenic
-
univentricular
- pharmacology
Reaction
Synonyms
biliverdin IXalpha reductase, biliverdin IXbeta reductase, biliverdin reductase, biliverdin reductase A, biliverdin reductase B, Biliverdin reductase-A, biliverdin-IXalpha reductase, BLVR subtype B, BLVRA, BLVRB, BV reductase, BVR, BVR-A, BVR-B, BVRA, BVRB, F-BVR, F420H2-dependent biliverdin reductase, hBVR, hBVR-A, reductase, biliverdin, Rv2074, slr1784
ECTree
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Crystallization
Crystallization on EC 1.3.1.24 - biliverdin reductase
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apo-, NADP+-bound and biliverdin-NADP+ complex forms of the enzyme, hanging drop vapor diffusion method, using 15% (w/v) PEG 4,000, 50 mM Tris-HCl (pH 7.25), 0.2 M sodium acetate and 0.2 mM Cymal-2
hanging drop vapor diffusion method, using 27% (w/v) PEG 3350, 0.2M MgCl2 and 0.1 M BisTris at pH 5.5
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apo-, NADP+-bound and biliverdin-NADP+ complex forms of the enzyme, hanging drop vapor diffusion method, using 15% (w/v) PEG 4,000, 50mM Tris-HCl (pH 7.25), 0.2M sodium acetate and 0.2mM Cymal-2
crystals of the biliverdin reductase obtained by sitting-drop vapour-diffusion method, enzyme diffraction data collected to 1.6 A, crystals belong to the orthorhombic space group P212121 with unit-cell parameters a=58.89, b=70.41, c=87.76 A
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an X-ray diffraction experiment using a native BVR crystal is performed on the BL38B1 beamline. The crystal belongs to the orthorhombic space group P2-1-2-1-2-1, with unit-cell parameters a = 58.8, b = 88.4, c = 132.6 A. A complete data set is collected to a resolution of 2.34 A
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apo-, NADP+-bound and biliverdin-NADP+ complex forms of the enzyme, hanging drop vapor diffusion method, using 15% (w/v) PEG 4,000, 50mM Tris-HCl (pH 7.25), 0.2M sodium acetate and 0.2mM Cymal-2