|Entry||Database: PDB / ID: 4l1w|
|Title||Crystal Structuer of Human 3-alpha Hydroxysteroid Dehydrogenase Type 3 in Complex with NADP+ and Progesterone|
|Components||Aldo-keto reductase family 1 member C2|
|Keywords||OXIDOREDUCTASE / ALPHA-BETA BARREL / HUMAN 3-ALPHA HSD3 / AKR / AKR1C2 / ALDO-KETO REDUCTASE / NADPH|
|Function / homology|
Function and homology information
indanol dehydrogenase / trans-1,2-dihydrobenzene-1,2-diol dehydrogenase / 3(or 17)alpha-hydroxysteroid dehydrogenase / trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity / indanol dehydrogenase activity / cellular response to prostaglandin D stimulus / 3alpha-hydroxysteroid 3-dehydrogenase / phenanthrene 9,10-monooxygenase activity / cellular response to jasmonic acid stimulus / 3alpha(or 20beta)-hydroxysteroid dehydrogenase ...indanol dehydrogenase / trans-1,2-dihydrobenzene-1,2-diol dehydrogenase / 3(or 17)alpha-hydroxysteroid dehydrogenase / trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity / indanol dehydrogenase activity / cellular response to prostaglandin D stimulus / 3alpha-hydroxysteroid 3-dehydrogenase / phenanthrene 9,10-monooxygenase activity / cellular response to jasmonic acid stimulus / 3alpha(or 20beta)-hydroxysteroid dehydrogenase / androstan-3-alpha,17-beta-diol dehydrogenase activity / androsterone dehydrogenase activity / ketosteroid monooxygenase activity / steroid dehydrogenase activity / Synthesis of bile acids and bile salts via 24-hydroxycholesterol / progesterone metabolic process / 17beta-estradiol 17-dehydrogenase / carboxylic acid binding / 17-beta-hydroxysteroid dehydrogenase (NAD+) activity / Oxidoreductases / daunorubicin metabolic process / oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor / doxorubicin metabolic process / bile acid binding / prostaglandin metabolic process / alditol:NADP+ 1-oxidoreductase activity / steroid metabolic process / Synthesis of bile acids and bile salts via 27-hydroxycholesterol / Synthesis of bile acids and bile salts via 7alpha-hydroxycholesterol / epithelial cell differentiation / digestion / positive regulation of protein kinase B signaling / G protein-coupled receptor signaling pathway / positive regulation of cell population proliferation / cytosol
Similarity search - Function
Aldo-keto reductase family 1 member C / Aldo/keto reductase family putative active site signature. / Aldo/keto reductase family signature 2. / Aldo/keto reductase, conserved site / NADP-dependent oxidoreductase domain / Aldo-keto reductase / NADP-dependent oxidoreductase domain / Aldo/keto reductase family / NADP-dependent oxidoreductase domain superfamily / TIM Barrel ...Aldo-keto reductase family 1 member C / Aldo/keto reductase family putative active site signature. / Aldo/keto reductase family signature 2. / Aldo/keto reductase, conserved site / NADP-dependent oxidoreductase domain / Aldo-keto reductase / NADP-dependent oxidoreductase domain / Aldo/keto reductase family / NADP-dependent oxidoreductase domain superfamily / TIM Barrel / Alpha-Beta Barrel / Alpha Beta
Similarity search - Domain/homology
NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE / PROGESTERONE / Aldo-keto reductase family 1 member C2
Similarity search - Component
|Biological species||Homo sapiens (human)|
|Method||X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.2 Å|
|Authors||Zhang, B. / Hu, X.-J. / Lin, S.-X.|
|Citation||Journal: J.Steroid Biochem.Mol.Biol. / Year: 2014|
Title: Human 3-alpha hydroxysteroid dehydrogenase type 3 (3 alpha-HSD3): The V54L mutation restricting the steroid alternative binding and enhancing the 20 alpha-HSD activity
Authors: Zhang, B. / Zhu, D.-W. / Hu, X.-J. / Zhou, M. / Shang, P. / Lin, S.-X.
|Structure viewer||Molecule: |
Downloads & links
A: Aldo-keto reductase family 1 member C2
B: Aldo-keto reductase family 1 member C2
A: Aldo-keto reductase family 1 member C2
B: Aldo-keto reductase family 1 member C2
|Noncrystallographic symmetry (NCS)||NCS domain: |
NCS domain segments:
Mass: 36956.363 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: AKR1C2 / Production host: Escherichia coli (E. coli)
References: UniProt: P52895, trans-1,2-dihydrobenzene-1,2-diol dehydrogenase, EC: 188.8.131.52
|#2: Chemical||#3: Chemical|
Mass: 314.462 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C21H30O2 / Comment: hormone*YM
|#4: Chemical||#5: Water|| ChemComp-HOH / |
|Experiment||Method: X-RAY DIFFRACTION / Number of used crystals: 1|
|Crystal||Density Matthews: 2.28 Å3/Da / Density % sol: 46.06 %|
|Crystal grow||Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 6 |
Details: 25% PEG3350, 0.1M Sodium Cacodylate, 0.2M Ammonium Sulfate, 0.8mM Progesterone, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K
|Diffraction||Mean temperature: 110 K|
|Diffraction source||Source: SYNCHROTRON / Site: APS / Beamline: 31-ID / Wavelength: 0.97931 Å|
|Detector||Type: RAYONIX MX225HE / Detector: CCD / Date: Oct 31, 2012|
|Radiation||Monochromator: Diamond(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray|
|Radiation wavelength||Wavelength: 0.97931 Å / Relative weight: 1|
|Reflection||Resolution: 2.2→21.5 Å / Num. obs: 32561 / % possible obs: 96.4 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.037|
|Reflection shell||Resolution: 2.2→2.32 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.056 / Num. unique all: 4701 / % possible all: 95.9|
|Refinement||Method to determine structure: MOLECULAR REPLACEMENT|
Starting model: 1J96
Resolution: 2.2→21.35 Å / Cor.coef. Fo:Fc: 0.955 / Cor.coef. Fo:Fc free: 0.921 / SU B: 4.264 / SU ML: 0.111 / Cross valid method: THROUGHOUT / ESU R: 0.282 / ESU R Free: 0.189 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
|Solvent computation||Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK|
|Displacement parameters||Biso mean: 11.739 Å2|
|Refinement step||Cycle: LAST / Resolution: 2.2→21.35 Å|
|Refine LS restraints|
|Refine LS restraints NCS|
Ens-ID: 1 / Number: 21131 / Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Rms dev position: 0.09 Å / Weight position: 0.05
|LS refinement shell||Resolution: 2.2→2.257 Å / Total num. of bins used: 20 |
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