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- PDB-1abn: THE CRYSTAL STRUCTURE OF THE ALDOSE REDUCTASE NADPH BINARY COMPLEX -
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Open data
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Basic information
Entry | Database: PDB / ID: 1abn | ||||||
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Title | THE CRYSTAL STRUCTURE OF THE ALDOSE REDUCTASE NADPH BINARY COMPLEX | ||||||
![]() | ALDOSE REDUCTASE | ||||||
![]() | OXIDOREDUCTASE | ||||||
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 | ![]() | ||||||
![]() | Borhani, D.W. / Harter, T.M. / Petrash, J.M. | ||||||
![]() | ![]() Title: The crystal structure of the aldose reductase.NADPH binary complex. Authors: Borhani, D.W. / Harter, T.M. / Petrash, J.M. #1: ![]() Title: Probing the Active Site of Aldose Reductase: Site-Directed Mutagenesis of Asp-43, Tyr-48, Lys-77, and His-110 Authors: Tarle, I. / Borhani, D.W. / Wilson, D.K. / Quiocho, F.A. / Petrash, J.M. #2: ![]() Title: Studies on Pig Aldose Reductase: Identification of an Essential Arginine in the Primary and Tertiary Structure of the Enzyme Authors: Kubiseski, T.J. / Green, N.C. / Borhani, D.W. / Flynn, T.G. #3: ![]() Title: Kinetic Alteration of Human Aldose Reductase by Mutagenesis of Cysteine Residues Authors: Petrash, J.M. / Harter, T. / Tarle, I. / Borhani, D. #4: ![]() Title: Involvement of Cysteine Residues in Catalysis and Inhibition of Human Aldose Reductase: Site Directed Mutagenesis of Cys-80,-298 and-303 Authors: Petrash, J.M. / Harter, T.M. / Devine, C.S. / Olins, P.O. / Bhatnagar, A. / Liu, S. / Srivastava, S.K. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 23.3 KB | Display | ![]() |
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PDB format | ![]() | 11.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 419.3 KB | Display | ![]() |
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Full document | ![]() | 420.3 KB | Display | |
Data in XML | ![]() | 1.7 KB | Display | |
Data in CIF | ![]() | 4.8 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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Unit cell |
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Components
#1: Protein | Mass: 35751.082 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-NDP / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.38 Å3/Da / Density % sol: 48.31 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 4 ℃ / pH: 6.2 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2.2 Å |
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Processing
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Refinement | Resolution: 2.4→6 Å / Rfactor obs: 0.286 | ||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.4→6 Å
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Refine LS restraints | *PLUS
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