|Entry||Database: PDB / ID: 3cv6|
|Title||The crystal structure of mouse 17-alpha hydroxysteroid dehydrogenase GG225.226PP mutant in complex with inhibitor and cofactor NADP+.|
|Components||Aldo-keto reductase family 1 member C21|
|Keywords||OXIDOREDUCTASE / Aldo-keto reductase / Hydroxysteroid Dehydrogenase / Ternary Complex / Hexestrol / Lipid metabolism / NADP / Phosphoprotein / Steroid metabolism|
|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-HXS / NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE / Aldo-keto reductase family 1 member C21
Similarity search - Component
|Biological species||Mus musculus (house mouse)|
|Method||X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.1 Å|
|Authors||Dhagat, U. / El-Kabbani, O.|
|Citation||Journal: Acta Crystallogr.,Sect.D / Year: 2009|
Title: Structure of the G225P/G226P mutant of mouse 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21) ternary complex: implications for the binding of inhibitor and substrate.
Authors: Dhagat, U. / Endo, S. / Mamiya, H. / Hara, A. / El-Kabbani, O.
|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
|Noncrystallographic symmetry (NCS)||NCS domain: |
NCS domain segments:
Component-ID: 1 / Ens-ID: 1 / Beg label comp-ID: MET / End label comp-ID: TYR / Refine code: 4 / Auth seq-ID: 1 - 323 / Label seq-ID: 1 - 323
Mass: 37004.707 Da / Num. of mol.: 2 / Mutation: G225P, G226P
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Akr1c21 / Plasmid: pkk223-3 / Production host: Escherichia coli (E. coli) / Strain (production host): JM109
References: UniProt: Q91WR5, 3(or 17)alpha-hydroxysteroid dehydrogenase
|#2: Chemical||#3: Chemical||#4: Chemical|
|#5: Water|| ChemComp-HOH / ||Sequence details||THERE ARE DIFFERENCES BETWEEN THE SEQRES AND THE SEQUENCE DATABASE. THIS IS A VARIANT AT THESE ...THERE ARE DIFFERENCE|
|Experiment||Method: X-RAY DIFFRACTION / Number of used crystals: 1|
|Crystal||Density Matthews: 2.94 Å3/Da / Density % sol: 58.15 %|
|Crystal grow||Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 7.5 |
Details: 0.1M Hepes, 10% PEG l6000, 5% 2-methyl-2,4-pentanediol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K
|Diffraction||Mean temperature: 100 K|
|Diffraction source||Source: ROTATING ANODE / Type: RIGAKU RU300 / Wavelength: 1.54179 Å|
|Detector||Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Jan 17, 2007 / Details: Mirrors|
|Radiation||Monochromator: Mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray|
|Radiation wavelength||Wavelength: 1.54179 Å / Relative weight: 1|
|Reflection||Resolution: 2.1→30 Å / Num. all: 46728 / Num. obs: 46635 / % possible obs: 99.8 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 2 / Redundancy: 4.01 % / Rmerge(I) obs: 0.0392 / Net I/σ(I): 16.7|
|Reflection shell||Resolution: 2.1→2.18 Å / Redundancy: 4.44 % / Rmerge(I) obs: 0.3672 / Mean I/σ(I) obs: 2.2 / % possible all: 100|
|Refinement||Method to determine structure: MOLECULAR REPLACEMENT|
Starting model: 2p5n
Resolution: 2.1→30 Å / Cor.coef. Fo:Fc: 0.961 / Cor.coef. Fo:Fc free: 0.932 / SU B: 5.418 / SU ML: 0.145 / Cross valid method: THROUGHOUT / σ(F): 1 / σ(I): 1 / ESU R: 0.221 / ESU R Free: 0.198 / Stereochemistry target values: MAXIMUM LIKELIHOOD
|Solvent computation||Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK|
|Displacement parameters||Biso mean: 36.98 Å2|
|Refinement step||Cycle: LAST / Resolution: 2.1→30 Å|
|Refine LS restraints|
|Refine LS restraints NCS|
Dom-ID: 1 / Auth asym-ID: A / Ens-ID: 1 / Number: 2619 / Refine-ID: X-RAY DIFFRACTION
|LS refinement shell||Resolution: 2.1→2.154 Å / Total num. of bins used: 20 |
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