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- PDB-1n5d: CRYSTAL STRUCTURE OF PORCINE TESTICULAR CARBONYL REDUCTASE/ 20BET... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1n5d | |||||||||
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Title | CRYSTAL STRUCTURE OF PORCINE TESTICULAR CARBONYL REDUCTASE/ 20BETA-HYDROXYSTEROID DEHYDROGENASE | |||||||||
![]() | CARBONYL REDUCTASE/20BETA-HYDROXYSTEROID DEHYDROGENASE | |||||||||
![]() | OXIDOREDUCTASE / SHORTCHAIN DEHYDROGENASE/REDUCTASE / MONOMER / NADP-COMPLEX | |||||||||
Function / homology | ![]() xenobiotic metabolic process => GO:0006805 / 15-hydroxyprostaglandin-D dehydrogenase (NADP+) / 15-hydroxyprostaglandin dehydrogenase (NADP+) / 15-hydroxyprostaglandin dehydrogenase (NADP+) activity / prostaglandin-E2 9-reductase / prostaglandin E2 9-reductase activity / carbonyl reductase (NADPH) / carbonyl reductase (NADPH) activity / vitamin K metabolic process / 15-hydroxyprostaglandin-D dehydrogenase (NADP+) activity / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Ghosh, D. | |||||||||
![]() | ![]() Title: Porcine Carbonyl Reductase: Structural Basis for a Functional Monomer in Short-Chain Dehydrogenases/Reductases Authors: Ghosh, D. / Sawicki, M. / Pletnev, V. / Erman, M. / Duax, W.L. / Ohno, S. / Nakajin, S. #1: ![]() Title: Crystallization and Preliminary X-Ray Diffraction Studies of a Mammalian Steroid Dehydrogenase Authors: Ghosh, D. / Erman, M. / Pangborn, W. / Duax, W.L. / Nakajin, S. / Ohno, S. / Shinoda, M. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 69.5 KB | Display | ![]() |
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PDB format | ![]() | 51.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 478.6 KB | Display | ![]() |
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Full document | ![]() | 485.6 KB | Display | |
Data in XML | ![]() | 8.5 KB | Display | |
Data in CIF | ![]() | 12.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
#1: Protein | Mass: 31600.076 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() References: UniProt: Q28960, 3alpha(or 20beta)-hydroxysteroid dehydrogenase |
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#2: Chemical | ChemComp-SO4 / |
#3: Chemical | ChemComp-NDP / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.24 Å3/Da / Density % sol: 45.17 % |
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Crystal grow | pH: 6 / Details: pH 6.00 |
Crystal grow | *PLUS Method: otherDetails: Ghosh, D., (1993) J. Steroid Biochem. Mol. Biol., 46, 103. |
-Data collection
Diffraction | Mean temperature: 280 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Nov 10, 1992 / Details: MONOCHROMATORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→100 Å / Num. obs: 10792 / % possible obs: 80 % / Observed criterion σ(I): 1 / Redundancy: 3 % / Biso Wilson estimate: 25 Å2 / Rmerge(I) obs: 0.066 / Net I/σ(I): 9.8 |
Reflection shell | Resolution: 2.3→2.5 Å / Redundancy: 2 % / % possible all: 52 |
Reflection | *PLUS Highest resolution: 2.3 Å / Lowest resolution: 55.2 Å / % possible obs: 80 % / Observed criterion σ(I): 1 / Redundancy: 3 % / Biso Wilson estimate: 25 Å2 |
Reflection shell | *PLUS % possible obs: 52 % / Redundancy: 2 % |
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Processing
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Refinement | Method to determine structure: ![]()
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.3→100 Å
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Refine LS restraints |
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Refinement | *PLUS Lowest resolution: 55.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |