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Yorodumi- PDB-1a27: HUMAN 17-BETA-HYDROXYSTEROID-DEHYDROGENASE TYPE 1 C-TERMINAL DELE... -
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-Basic information
Entry | Database: PDB / ID: 1a27 | ||||||
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Title | HUMAN 17-BETA-HYDROXYSTEROID-DEHYDROGENASE TYPE 1 C-TERMINAL DELETION MUTANT COMPLEXED WITH ESTRADIOL AND NADP+ | ||||||
Components | 17-BETA-HYDROXYSTEROID-DEHYDROGENASE | ||||||
Keywords | DEHYDROGENASE / 17-BETA-HYDROXYSTEROID / MUTANT / ESTRADIOL / NADP | ||||||
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 / dihydrotestosterone 17-beta-dehydrogenase activity / testosterone biosynthetic process / 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 / dihydrotestosterone 17-beta-dehydrogenase activity / testosterone biosynthetic process / testosterone dehydrogenase (NAD+) activity / testosterone 17-beta-dehydrogenase (NADP+) activity / 17beta-estradiol 17-dehydrogenase / estradiol 17-beta-dehydrogenase [NAD(P)+] activity / steroid biosynthetic process / estrogen metabolic process / NADP+ binding / lysosome organization / The canonical retinoid cycle in rods (twilight vision) / small molecule binding / catalytic activity / adipose tissue development / skeletal muscle tissue development / steroid binding / bone development / NADP binding / gene expression / protein homodimerization activity / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å | ||||||
Authors | Mazza, C. / Breton, R. / Housset, D. / Fontecilla-Camps, J.-C. | ||||||
Citation | Journal: Thesis, Universite Joseph Fourier / Year: 1997 Title: Human Type I 17Beta-Hydroxysteroid Dehydrogenase: Site Directed Mutagenesis and X-Ray Crystallography Structure-Function Analysis Authors: Mazza, C. #1: Journal: J.Biol.Chem. / Year: 1998 Title: Unusual Charge Stabilization of Nadp+ in 17Beta-Hydroxysteroid Dehydrogenase Authors: Mazza, C. / Breton, R. / Housset, D. / Fontecilla-Camps, J.C. #2: Journal: Structure / Year: 1996 Title: The Structure of a Complex of Human 17Beta-Hydroxysteroid Dehydrogenase with Estradiol and Nadp+ Identifies Two Principal Targets for the Design of Inhibitors Authors: Breton, R. / Housset, D. / Mazza, C. / Fontecilla-Camps, J.C. #3: Journal: Structure / Year: 1995 Title: Structure of Human Estrogenic 17 Beta-Hydroxysteroid Dehydrogenase at 2.20 A Resolution Authors: Ghosh, D. / Pletnev, V.Z. / Zhu, D.W. / Wawrzak, Z. / Duax, W.L. / Pangborn, W. / Labrie, F. / Lin, S.X. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1a27.cif.gz | 73.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1a27.ent.gz | 53.8 KB | Display | PDB format |
PDBx/mmJSON format | 1a27.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1a27_validation.pdf.gz | 1 MB | Display | wwPDB validaton report |
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Full document | 1a27_full_validation.pdf.gz | 1.1 MB | Display | |
Data in XML | 1a27_validation.xml.gz | 16 KB | Display | |
Data in CIF | 1a27_validation.cif.gz | 22.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/a2/1a27 ftp://data.pdbj.org/pub/pdb/validation_reports/a2/1a27 | HTTPS FTP |
-Related structure data
Related structure data | 1fdtS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 31473.318 Da / Num. of mol.: 1 / Mutation: C-TERMINAL DELETION (290 - 327) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Cell line: SPODOPTERA FRUGIPERDA / Cellular location: CYTOPLASM / Plasmid: PVL1393 / Cell line (production host): SPODOPTERA FRUGIPERDA / Cellular location (production host): CYTOPLASM / Production host: unidentified baculovirus References: UniProt: P14061, 17beta-estradiol 17-dehydrogenase |
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#2: Chemical | ChemComp-EST / |
#3: Chemical | ChemComp-NAP / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.13 Å3/Da / Density % sol: 42 % |
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Crystal grow | pH: 7.1 Details: PROTEIN WAS CRYSTALLIZED FROM 12-16 % PEG4000, 100 MM HEPES PH 7.1, 0.5 MM ESTRADIOL, 200 MM NACL, 100MM MGCL2, 2.2 MM DECYL-BETA-D-MALTOSIDE; THEN SOAKED IN 30 % PEG 4000, 100 MM HEPES PH 7. ...Details: PROTEIN WAS CRYSTALLIZED FROM 12-16 % PEG4000, 100 MM HEPES PH 7.1, 0.5 MM ESTRADIOL, 200 MM NACL, 100MM MGCL2, 2.2 MM DECYL-BETA-D-MALTOSIDE; THEN SOAKED IN 30 % PEG 4000, 100 MM HEPES PH 7.1, 100 MM MGCL2, 0.5 MM ESTRADIOL, 1 MM NADP+ |
-Data collection
Diffraction | Mean temperature: 130 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: BM02 / Wavelength: 0.9827 |
Detector | Type: ESRF / Detector: CCD / Date: Feb 1, 1996 / Details: MIRRORS |
Radiation | Monochromator: MIRRORS / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9827 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→40 Å / Num. obs: 15988 / % possible obs: 70.6 % / Observed criterion σ(I): 0 / Redundancy: 2.83 % / Rsym value: 0.034 |
Reflection shell | Resolution: 1.9→2 Å / Redundancy: 1.12 % / Rsym value: 0.162 / % possible all: 34.5 |
-Processing
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1FDT Resolution: 1.9→10 Å / σ(F): 2
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Displacement parameters | Biso mean: 32.83 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→10 Å
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Refine LS restraints |
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