|Entry||Database: PDB / ID: 2hej|
|Title||Crystal structure of 17alpha-hydroxysteroid dehydrogenase in complex with NADP(H) in a closed conformation|
|Components||Aldo-keto reductase family 1, member C21|
|Keywords||OXIDOREDUCTASE / 17a-HSD / AKR1C21 / AKR / aldo-keto reductase / HSD / hydroxysteroid dehydrogenase / closed conformation|
|Function / homology|
Function and homology information
17-beta-ketosteroid reductase activity / steroid dehydrogenase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor / chlordecone reductase activity / androsterone dehydrogenase (B-specific) activity / 3(or 17)alpha-hydroxysteroid dehydrogenase / trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity / 17-beta-hydroxysteroid dehydrogenase (NADP+) activity / 5alpha-androstane-3beta,17beta-diol dehydrogenase activity / phenanthrene 9,10-monooxygenase activity / cellular response to jasmonic acid stimulus ...17-beta-ketosteroid reductase activity / steroid dehydrogenase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor / chlordecone reductase activity / androsterone dehydrogenase (B-specific) activity / 3(or 17)alpha-hydroxysteroid dehydrogenase / trans-1,2-dihydrobenzene-1,2-diol dehydrogenase activity / 17-beta-hydroxysteroid dehydrogenase (NADP+) activity / 5alpha-androstane-3beta,17beta-diol dehydrogenase activity / phenanthrene 9,10-monooxygenase activity / cellular response to jasmonic acid stimulus / androsterone dehydrogenase activity / ketosteroid monooxygenase activity / steroid dehydrogenase activity / progesterone metabolic process / carboxylic acid binding / aldo-keto reductase (NADP) activity / lithocholic acid binding / steroid biosynthetic process / Oxidoreductases; Acting on the CH-OH group of donors; With NAD+ or NADP+ as acceptor / daunorubicin metabolic process / oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor / doxorubicin metabolic process / retinal dehydrogenase activity / NADP+ binding / bile acid binding / prostaglandin metabolic process / alditol:NADP+ 1-oxidoreductase activity / steroid metabolic process / NADPH binding / steroid binding / cytosol
Similarity search - Function
Aldo-keto reductase family 1 member C / 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
BETA-MERCAPTOETHANOL / Chem-NDP / Aldo-keto reductase family 1 member C21 / Aldo-keto reductase family 1 member C21
Similarity search - Component
|Biological species||Mus musculus (house mouse)|
|Method||X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.35 Å|
|Authors||Faucher, F. / Pereira de Jesus-Tran, K. / Cantin, L. / Luu-the, V. / Labrie, F. / Breton, R.|
|Citation||Journal: J.Mol.Biol. / Year: 2006|
Title: Crystal Structures of Mouse 17alpha-Hydroxysteroid Dehydrogenase (Apoenzyme and Enzyme-NADP(H) Binary Complex): Identification of Molecular Determinants Responsible for the Unique 17alpha- ...Title: Crystal Structures of Mouse 17alpha-Hydroxysteroid Dehydrogenase (Apoenzyme and Enzyme-NADP(H) Binary Complex): Identification of Molecular Determinants Responsible for the Unique 17alpha-reductive Activity of this Enzyme.
Authors: Faucher, F. / Pereira de Jesus-Tran, K. / Cantin, L. / Luu-The, V. / Labrie, F. / Breton, R.
|Structure viewer||Molecule: |
Downloads & links
A: Aldo-keto reductase family 1, member C21
B: Aldo-keto reductase family 1, member C21
A: Aldo-keto reductase family 1, member C21
B: Aldo-keto reductase family 1, member C21
-Protein , 1 types, 2 molecules A
Mass: 36924.578 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Akr1c21 / Plasmid: pGEX1lT / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pLys / References: UniProt: Q9CX32, UniProt: Q91WR5*PLUS
-Non-polymers , 5 types, 767 molecules
|#2: Chemical||#3: Chemical|
|#4: Chemical||#5: Chemical|
Mass: 118.174 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C6H14O2 / Comment: precipitant*YM
|#6: Water|| ChemComp-HOH / |
|Experiment||Method: X-RAY DIFFRACTION / Number of used crystals: 1|
|Crystal||Density Matthews: 2.33 Å3/Da / Density % sol: 47.23 %|
|Crystal grow||Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7.8 |
Details: 18% PEG-6000, 0.1M HEPES, 5% MPD, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|Diffraction||Mean temperature: 100 K|
|Diffraction source||Source: SYNCHROTRON / Site: APS / Beamline: 17-ID / Wavelength: 1 Å|
|Detector||Type: MAR CCD 165 mm / Detector: CCD / Date: Mar 28, 2006|
|Radiation||Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray|
|Radiation wavelength||Wavelength: 1 Å / Relative weight: 1|
|Reflection||Resolution: 1.35→38.13 Å / Num. all: 142410 / Num. obs: 142410 / % possible obs: 93.3 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Biso Wilson estimate: 17.891 Å2 / Rmerge(I) obs: 0.051 / Net I/σ(I): 15.88|
|Phasing MR||Rfactor: 0.362 / Cor.coef. Fo:Fc: 0.647 |
|Refinement||Method to determine structure: MOLECULAR REPLACEMENT|
Starting model: pdb entry 2HE8
Resolution: 1.35→38.13 Å / Rfactor Rfree error: 0.003 / FOM work R set: 0.855 / Data cutoff high absF: 1548498.5 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
|Solvent computation||Solvent model: FLAT MODEL / Bsol: 56.545 Å2 / ksol: 0.385 e/Å3|
|Displacement parameters||Biso mean: 15.6 Å2|
|Refinement step||Cycle: LAST / Resolution: 1.35→38.13 Å|
|Refine LS restraints|
|LS refinement shell|
Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 50
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