|Entry||Database: PDB / ID: 2ipg|
|Title||Crystal structure of 17alpha-hydroxysteroid dehydrogenase mutant K31A in complex with NADP+ and epi-testosterone|
|Keywords||OXIDOREDUCTASE / 17a-HSD / AKR1C21 / AKR / aldo-keto reductase / HSD / hydroxysteroid dehydrogenase / open conformation / epi-testosterone|
|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-FFA / 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: 1.9 Å|
|Authors||Faucher, F. / Cantin, L. / Pereira de Jesus-Tran, K. / Lemieux, M. / 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: 3(17)alpha-hydroxysteroid dehydrogenase
B: 3(17)alpha-hydroxysteroid dehydrogenase
|Noncrystallographic symmetry (NCS)||NCS oper: |
-Protein , 1 types, 2 molecules A
Mass: 36404.930 Da / Num. of mol.: 2 / Mutation: K31A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Akr1c21 / Plasmid: pGEX1lT / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3)pLys
References: UniProt: Q91WR5, Oxidoreductases; Acting on the CH-OH group of donors; With NAD+ or NADP+ as acceptor, 3(or 17)alpha-hydroxysteroid dehydrogenase
-Non-polymers , 5 types, 492 molecules
Mass: 743.405 Da / Num. of mol.: 2 / Mutation: K31A / Source method: obtained synthetically / Formula: C21H28N7O17P3
Mass: 288.424 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C19H28O2 / Comment: inhibitor, antagonist, hormone*YM
|#5: Chemical||#6: Water|| ChemComp-HOH / |
|Experiment||Method: X-RAY DIFFRACTION / Number of used crystals: 1|
|Crystal||Density Matthews: 2.31 Å3/Da / Density % sol: 46.66 %|
|Crystal grow||Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6.4 |
Details: PEG-4000 24%, 0.1M MES, O.1M Li2SO4, pH 6.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K
|Radiation wavelength||Wavelength: 1.5418 Å / Relative weight: 1|
|Reflection||Resolution: 2→19.56 Å / Num. all: 45224 / Num. obs: 43065 / % possible obs: 94.7 % / Observed criterion σ(I): 0 / Redundancy: 3.9 % / Biso Wilson estimate: 9.5 Å2 / Rmerge(I) obs: 0.117 / Rsym value: 0.172 / Net I/σ(I): 7.12|
|Reflection shell||Resolution: 2→2.1 Å / Redundancy: 4 % / Rmerge(I) obs: 0.191 / Mean I/σ(I) obs: 4.93 / Rsym value: 0.262 / % possible all: 92.1|
|Refinement||Method to determine structure: MOLECULAR REPLACEMENT|
Starting model: 2IPF
Resolution: 1.9→19.55 Å / Rfactor Rfree error: 0.004 / Data cutoff high absF: 1754729.91 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
|Solvent computation||Solvent model: FLAT MODEL / Bsol: 43.1045 Å2 / ksol: 0.337572 e/Å3|
|Displacement parameters||Biso mean: 17.2 Å2|
|Refinement step||Cycle: LAST / Resolution: 1.9→19.55 Å|
|Refine LS restraints|
|Refine LS restraints NCS||NCS model details: CONSTR|
|LS refinement shell||Resolution: 1.9→2.02 Å / Rfactor Rfree error: 0.012 / Total num. of bins used: 6 |
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