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Yorodumi- PDB-1fdv: HUMAN 17-BETA-HYDROXYSTEROID-DEHYDROGENASE TYPE 1 MUTANT H221L CO... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1fdv | ||||||
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Title | HUMAN 17-BETA-HYDROXYSTEROID-DEHYDROGENASE TYPE 1 MUTANT H221L COMPLEXED WITH NAD+ | ||||||
Components | 17-BETA-HYDROXYSTEROID DEHYDROGENASE | ||||||
Keywords | DEHYDROGENASE / 17-BETA-HYDROXYSTEROID / MUTANT / NAD | ||||||
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 dehydrogenase (NAD+) activity / testosterone biosynthetic process ...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 dehydrogenase (NAD+) activity / testosterone biosynthetic process / 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 / adipose tissue development / catalytic activity / skeletal muscle tissue development / steroid binding / bone development / gene expression / NADP binding / protein homodimerization activity / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.1 Å | ||||||
Authors | Mazza, C. / Breton, R. / Housset, D. / Fontecilla-Camps, J.-C. | ||||||
Citation | 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. #1: 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. #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 | 1fdv.cif.gz | 197.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fdv.ent.gz | 157.3 KB | Display | PDB format |
PDBx/mmJSON format | 1fdv.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fd/1fdv ftp://data.pdbj.org/pub/pdb/validation_reports/fd/1fdv | HTTPS FTP |
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-Related structure data
Related structure data | 1fduC 1fdwC 1fdtS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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-Components
#1: Protein | Mass: 34948.961 Da / Num. of mol.: 4 / Mutation: H221L Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Cellular location: CYTOPLASM / Plasmid: PVL1393 / Cellular location (production host): CYTOPLASM / Production host: Spodoptera frugiperda (fall armyworm) References: UniProt: P14061, 17beta-estradiol 17-dehydrogenase #2: Chemical | ChemComp-SO4 / #3: Chemical | ChemComp-NAD / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.96 Å3/Da / Density % sol: 69 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 6.3 Details: PROTEIN WAS CRYSTALLIZED FROM 2 M AMMONIUM SULFATE, 100 MM SODIUM PHOSPHATE BUFFER PH 6.3, 1 MM NAD+, 100 MM NACL; THEN SOAKED IN 27 % GLYCEROL, 2.3 M AMMONIUM SULFATE, 100 MM SODIUM ...Details: PROTEIN WAS CRYSTALLIZED FROM 2 M AMMONIUM SULFATE, 100 MM SODIUM PHOSPHATE BUFFER PH 6.3, 1 MM NAD+, 100 MM NACL; THEN SOAKED IN 27 % GLYCEROL, 2.3 M AMMONIUM SULFATE, 100 MM SODIUM PHOSPHATE BUFFER PH 6.1, 80 MM NACL, 1 MM NAD+ | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.5 / Method: unknown | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 130 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: BM02 / Wavelength: 0.9795 |
Detector | Type: ESRF / Detector: CCD / Date: Nov 1, 1995 / Details: MIRRORS |
Radiation | Monochromator: MIRRORS / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 |
Reflection | Resolution: 3→40 Å / Num. obs: 56921 / % possible obs: 91.6 % / Observed criterion σ(I): 0 / Redundancy: 3.61 % / Rsym value: 0.146 |
Reflection shell | Resolution: 3.1→3.2 Å / Redundancy: 3.94 % / Rsym value: 0.418 / % possible all: 98.5 |
Reflection | *PLUS Rmerge(I) obs: 0.146 |
Reflection shell | *PLUS % possible obs: 98.5 % / Rmerge(I) obs: 0.418 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1FDT Resolution: 3.1→10 Å / σ(F): 2
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Displacement parameters | Biso mean: 25.33 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.1→10 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.219 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |