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- PDB-1pwl: Crystal structure of human Aldose Reductase complexed with NADP a... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1pwl | ||||||
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Title | Crystal structure of human Aldose Reductase complexed with NADP and Minalrestat | ||||||
![]() | aldose reductase | ||||||
![]() | OXIDOREDUCTASE / ALDOSE REDUCTASE / ATOMIC RESOLUTION / TERNARY COMPLEX / INHIBITOR BINDING | ||||||
Function / homology | ![]() glyceraldehyde oxidoreductase activity / Fructose biosynthesis / fructose biosynthetic process / L-glucuronate reductase activity / glycerol dehydrogenase (NADP+) activity / D/L-glyceraldehyde reductase / aldose reductase / C21-steroid hormone biosynthetic process / Pregnenolone biosynthesis / NADP-retinol dehydrogenase ...glyceraldehyde oxidoreductase activity / Fructose biosynthesis / fructose biosynthetic process / L-glucuronate reductase activity / glycerol dehydrogenase (NADP+) activity / D/L-glyceraldehyde reductase / aldose reductase / C21-steroid hormone biosynthetic process / Pregnenolone biosynthesis / NADP-retinol dehydrogenase / allyl-alcohol dehydrogenase / allyl-alcohol dehydrogenase activity / L-ascorbic acid biosynthetic process / metanephric collecting duct development / prostaglandin H2 endoperoxidase reductase activity / regulation of urine volume / all-trans-retinol dehydrogenase (NADP+) activity / renal water homeostasis / daunorubicin metabolic process / doxorubicin metabolic process / epithelial cell maturation / retinal dehydrogenase activity / aldose reductase (NADPH) activity / retinoid metabolic process / cellular hyperosmotic salinity response / carbohydrate metabolic process / electron transfer activity / negative regulation of apoptotic process / extracellular space / extracellular exosome / nucleoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | El-Kabbani, O. / Darmanin, C. / Schneider, T.R. / Hazemann, I. / Ruiz, F. / Oka, M. / Joachimiak, A. / Schulze-Briese, C. / Tomizaki, T. / Mitschler, A. / Podjarny, A. | ||||||
![]() | ![]() Title: Ultrahigh resolution drug design. II. Atomic resolution structures of human aldose reductase holoenzyme complexed with Fidarestat and Minalrestat: implications for the binding of cyclic imide inhibitors Authors: El-Kabbani, O. / Darmanin, C. / Schneider, T.R. / Hazemann, I. / Ruiz, F. / Oka, M. / Joachimiak, A. / Schulze-Briese, C. / Tomizaki, T. / Mitschler, A. / Podjarny, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 169.5 KB | Display | ![]() |
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PDB format | ![]() | 132 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related 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: 35898.340 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-BFI / |
#3: Chemical | ChemComp-NAP / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.64 Å3/Da / Density % sol: 24.9 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 5 Details: PEG 6000, ammonium citrate, pH 5, VAPOR DIFFUSION, HANGING DROP, temperature 277K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K | |||||||||
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Diffraction source | Source: ![]() ![]() ![]() | |||||||||
Detector | Type: CUSTOM-MADE / Detector: CCD / Date: Jun 30, 2001 | |||||||||
Radiation | Monochromator: MIRRORS / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||
Radiation wavelength |
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Reflection | Resolution: 1.1→50 Å / Num. all: 115145 / Num. obs: 115145 / % possible obs: 92.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.63 % / Rmerge(I) obs: 0.041 / Net I/σ(I): 25.6 | |||||||||
Reflection shell | Resolution: 1.1→1.61 Å / Redundancy: 3.13 % / Rmerge(I) obs: 0.0921 / Mean I/σ(I) obs: 11.75 / % possible all: 81.5 | |||||||||
Reflection | *PLUS % possible obs: 92.6 % / Rmerge(I) obs: 0.041 | |||||||||
Reflection shell | *PLUS % possible obs: 81.5 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: ALDOSE REDUCTASE HOLOENZYME Resolution: 1.1→10 Å / Num. parameters: 28902 / Num. restraintsaints: 36371 / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: ENGH & HUBER
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Displacement parameters | Biso mean: 13.4 Å2 | |||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.035 Å / Num. disordered residues: 95 / Occupancy sum hydrogen: 2390.21 / Occupancy sum non hydrogen: 2967.93 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.1→10 Å
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Refine LS restraints |
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Software | *PLUS Name: SHELXL / Version: 97 / Classification: refinement | |||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.1 Å / Lowest resolution: 10 Å / Rfactor Rfree: 0.124 / Rfactor Rwork: 0.099 | |||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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