|Entry||Database: PDB / ID: 4jq2|
|Title||AKR1C2 complex with sulindac|
|Components||Aldo-keto reductase family 1 member C2|
|Keywords||Oxidoreductase/Oxidoreductase inhibitor / OXIDOREDUCTASE / Oxidoreductase-Oxidoreductase inhibitor complex|
|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 / PHOSPHATE ION / Chem-SUZ / L(+)-TARTARIC ACID / Aldo-keto reductase family 1 member C2
Similarity search - Component
|Biological species||Homo sapiens (human)|
|Method||X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.75 Å|
|Authors||Yosaatmadja, Y. / Flanagan, J.U. / Squire, C.J.|
|Citation||Journal: To be Published|
Title: Structural basis of NSAID selectivity for the aldo-keto reductase 1C family
Authors: Yosaatmadja, Y. / Flanagan, J.U. / Squire, C.J.
|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
|Components on special symmetry positions|
-Protein , 1 types, 2 molecules A
Mass: 37857.406 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: AKR1C2, DDH2 / Plasmid: pET22b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)
References: UniProt: P52895, Oxidoreductases, trans-1,2-dihydrobenzene-1,2-diol dehydrogenase, EC: 18.104.22.168
-Non-polymers , 6 types, 342 molecules
|#2: Chemical|| ChemComp-SUZ / [(|
|#3: Chemical||#4: Chemical|
|#5: Chemical|| ChemComp-TLA / ||#6: Chemical|| ChemComp-PO4 / ||#7: Water|| ChemComp-HOH / |
|Experiment||Method: X-RAY DIFFRACTION / Number of used crystals: 1|
|Crystal||Density Matthews: 2.67 Å3/Da / Density % sol: 53.91 %|
|Crystal grow||Temperature: 291 K / Method: vapor diffusion, sitting drop|
Details: 20% PEG 3350, 0.2 M diammonium-L-tartrate, VAPOR DIFFUSION, SITTING DROP, temperature 291K
|Diffraction||Mean temperature: 100 K|
|Diffraction source||Source: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.9537 Å|
|Detector||Type: ADSC QUANTUM 315r / Detector: CCD / Date: Sep 29, 2012|
|Radiation||Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray|
|Radiation wavelength||Wavelength: 0.9537 Å / Relative weight: 1|
|Reflection||Resolution: 1.75→106.1 Å / Num. all: 80393 / Num. obs: 80393 / % possible obs: 99.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 19.1 % / Biso Wilson estimate: 26.1 Å2|
|Reflection shell||Resolution: 1.75→1.84 Å / % possible all: 95.7|
|Refinement||Method to determine structure: MOLECULAR REPLACEMENT|
Starting model: inhouse unliganded
Resolution: 1.75→19.79 Å / Cor.coef. Fo:Fc: 0.973 / Cor.coef. Fo:Fc free: 0.954 / SU B: 6.415 / SU ML: 0.087 / Cross valid method: THROUGHOUT / ESU R: 0.137 / ESU R Free: 0.108 / 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: 34.878 Å2|
|Refinement step||Cycle: LAST / Resolution: 1.75→19.79 Å|
|Refine LS restraints|
|LS refinement shell||Resolution: 1.75→1.795 Å / Total num. of bins used: 20 |
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