|Entry||Database: PDB / ID: 1qyv|
|Title||Crystal structure of human estrogenic 17beta-hydroxysteroid dehydrogenase complex with NADP|
|Components||Estradiol 17 beta-dehydrogenase 1|
|Keywords||OXIDOREDUCTASE / 17bHSD1-cofactor complex|
|Function / homology|
Function and homology information
estradiol binding / 3(or 17)beta-hydroxysteroid dehydrogenase / 17-beta-hydroxysteroid dehydrogenase (NADP+) activity / estrogen biosynthetic process / testosterone dehydrogenase [NAD(P)] activity / cellular response to metal ion / Estrogen biosynthesis / estradiol 17-beta-dehydrogenase [NAD(P)] activity / dihydrotestosterone 17-beta-dehydrogenase activity / testosterone dehydrogenase (NAD+) activity ...estradiol binding / 3(or 17)beta-hydroxysteroid dehydrogenase / 17-beta-hydroxysteroid dehydrogenase (NADP+) activity / estrogen biosynthetic process / testosterone dehydrogenase [NAD(P)] activity / cellular response to metal ion / Estrogen biosynthesis / estradiol 17-beta-dehydrogenase [NAD(P)] activity / dihydrotestosterone 17-beta-dehydrogenase activity / testosterone dehydrogenase (NAD+) activity / testosterone biosynthetic process / testosterone 17-beta-dehydrogenase (NADP+) activity / 17beta-estradiol 17-dehydrogenase / 17-beta-hydroxysteroid dehydrogenase (NAD+) activity / steroid biosynthetic process / NADP+ binding / estrogen metabolic process / The canonical retinoid cycle in rods (twilight vision) / small molecule binding / catalytic activity / steroid binding / bone development / NADP binding / oxidoreductase activity / protein homodimerization activity / cytosol / cytoplasm
Similarity search - Function
17beta-dehydrogenase / short chain dehydrogenase / Short-chain dehydrogenase/reductase, conserved site / Short-chain dehydrogenases/reductases family signature. / Short-chain dehydrogenase/reductase SDR / NAD(P)-binding Rossmann-like Domain / NAD(P)-binding domain superfamily / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE / 17-beta-hydroxysteroid dehydrogenase type 1
Similarity search - Component
|Biological species||Homo sapiens (human)|
|Method||X-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 1.81 Å|
|Authors||Shi, R. / Lin, S.X.|
|Citation||Journal: J.Biol.Chem. / Year: 2004|
Title: Cofactor hydrogen bonding onto the protein main chain is conserved in the short chain dehydrogenase/reductase family and contributes to nicotinamide orientation.
Authors: Shi, R. / Lin, S.X.
|Structure viewer||Molecule: |
Downloads & links
A: Estradiol 17 beta-dehydrogenase 1
A: Estradiol 17 beta-dehydrogenase 1
A: Estradiol 17 beta-dehydrogenase 1
|Details||The second part of the biological assembly is genearated by the two fold axis: -X, Y, -Z.|
|#1: Protein|| |
Mass: 34887.828 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Tissue: placenta
References: UniProt: P14061, 17beta-estradiol 17-dehydrogenase
|#2: Chemical|| ChemComp-NAP / |
|#3: Chemical|| ChemComp-GOL / |
|#4: Water|| ChemComp-HOH / |
|Experiment||Method: X-RAY DIFFRACTION / Number of used crystals: 1|
|Crystal||Density Matthews: 2.3 Å3/Da / Density % sol: 46.43 %|
|Crystal grow||Temperature: 300 K / Method: vapor diffusion, hanging drop / pH: 7.5 |
Details: PEG4000, magnisum chloride, beta-octylglucoside, HEPES, glycerol, soaking with NADP, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 300K
|Diffraction||Mean temperature: 100 K|
|Diffraction source||Source: SYNCHROTRON / Site: NSLS / Beamline: X8C / Wavelength: 0.9795 Å|
|Detector||Type: ADSC QUANTUM 4 / Detector: CCD / Date: Apr 15, 2000 / Details: mirrors|
|Radiation||Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray|
|Radiation wavelength||Wavelength: 0.9795 Å / Relative weight: 1|
|Reflection||Resolution: 1.81→40 Å / Num. obs: 28701 / % possible obs: 98.1 % / Observed criterion σ(I): 2 / Redundancy: 3.55 % / Biso Wilson estimate: 21.5 Å2 / Rmerge(I) obs: 0.049|
|Reflection shell||Resolution: 1.81→1.87 Å / Redundancy: 2.82 % / Rmerge(I) obs: 0.397 / Mean I/σ(I) obs: 2 / Num. unique all: 2669 / % possible all: 92.2|
|Refinement||Method to determine structure: FOURIER SYNTHESIS|
Starting model: PDB entry 1JTV
Resolution: 1.81→10 Å / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 1 / Stereochemistry target values: Engh & Huber
|Displacement parameters||Biso mean: 35.3 Å2|
|Refinement step||Cycle: LAST / Resolution: 1.81→10 Å|
|Refine LS restraints|
|LS refinement shell||Resolution: 1.81→1.887 Å|
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