|Entry||Database: PDB / ID: 2ipj|
|Title||Crystal structure of h3alpha-hydroxysteroid dehydrogenase type 3 mutant Y24A in complex with NADP+ and epi-testosterone|
|Components||Aldo-keto reductase family 1 member C2|
|Keywords||OXIDOREDUCTASE / 3a-HSD / AKR1C21 / AKR / aldo-keto reductase / HSD / hydroxysteroid dehydrogenase / open conformation / epi-testosterone|
|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
BETA-MERCAPTOETHANOL / Chem-FFA / NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE / Aldo-keto reductase family 1 member C2
Similarity search - Component
|Biological species||Homo sapiens (human)|
|Method||X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.8 Å|
|Authors||Faucher, F. / Cantin, L. / Pereira de Jesus-Tran, K. / Luu-the, V. / Labrie, F. / Breton, R.|
|Citation||Journal: J.Mol.Biol. / Year: 2007|
Title: Mouse 17alpha-Hydroxysteroid Dehydrogenase (AKR1C21) Binds Steroids Differently from other Aldo-keto Reductases: Identification and Characterization of Amino Acid Residues Critical for Substrate Binding.
Authors: Faucher, F. / Cantin, L. / Pereira de Jesus-Tran, K. / Lemieux, M. / Luu-The, V. / Labrie, F. / Breton, R.
|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|
|Noncrystallographic symmetry (NCS)||NCS oper: |
-Protein , 1 types, 2 molecules A
Mass: 36447.891 Da / Num. of mol.: 2 / Mutation: Y24A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: AKR1C2 / Plasmid: pGEX1lT / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pLys
References: UniProt: P52895, Oxidoreductases, trans-1,2-dihydrobenzene-1,2-diol dehydrogenase, EC: 22.214.171.124
-Non-polymers , 6 types, 630 molecules
|#2: Chemical||#3: Chemical||#4: Chemical|
Mass: 288.424 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C19H28O2 / Comment: inhibitor, antagonist, hormone*YM
|#5: Chemical||#6: Chemical|
|#7: Water|| ChemComp-HOH / |
|Experiment||Method: X-RAY DIFFRACTION / Number of used crystals: 1|
|Crystal||Density Matthews: 2.82 Å3/Da / Density % sol: 56.38 %|
|Crystal grow||Temperature: 277 K / Method: hanging drop / pH: 5.6 |
Details: PEG-4000 22%, 0.1M NaCitrate, pH 5.6, hanging drop, temperature 277K
|Diffraction source||Source: SYNCHROTRON / Site: ESRF / Beamline: BM30A / Wavelength: 1 Å|
|Detector||Type: MAR CCD 130 mm / Detector: CCD / Date: Dec 3, 2005|
|Radiation wavelength||Wavelength: 1 Å / Relative weight: 1|
|Reflection||Resolution: 1.8→19.98 Å / Num. all: 75962 / Num. obs: 75736 / % possible obs: 99.7 % / Observed criterion σ(I): 0 / Redundancy: 7.4 % / Biso Wilson estimate: 29.947 Å2 / Rmerge(I) obs: 0.068 / Rsym value: 0.066 / Net I/σ(I): 18.29|
|Reflection shell||Resolution: 1.8→1.9 Å / Redundancy: 7.4 % / Rmerge(I) obs: 0.278 / Mean I/σ(I) obs: 4.4 / Num. measured obs: 82991 / Num. unique all: 11281 / Rsym value: 0.458 / % possible all: 97.6|
|Refinement||Method to determine structure: MOLECULAR REPLACEMENT|
Starting model: 2HDJ
Resolution: 1.8→19.98 Å / Rfactor Rfree error: 0.004 / FOM work R set: 0.846 / Data cutoff high absF: 8881042 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
|Solvent computation||Solvent model: FLAT MODEL / Bsol: 51.737 Å2 / ksol: 0.339 e/Å3|
|Displacement parameters||Biso mean: 28.6 Å2|
|Refinement step||Cycle: LAST / Resolution: 1.8→19.98 Å|
|Refine LS restraints|
|LS refinement shell|
Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 50
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