+Open data
-Basic information
Entry | Database: PDB / ID: 1el3 | ||||||
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Title | HUMAN ALDOSE REDUCTASE COMPLEXED WITH IDD384 INHIBITOR | ||||||
Components | ALDOSE REDUCTASE | ||||||
Keywords | OXIDOREDUCTASE / ALDOSE REDUCTASE / INHIBITION / DIABETES | ||||||
Function / homology | Function and homology information 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 / L-ascorbic acid biosynthetic process / allyl-alcohol dehydrogenase / allyl-alcohol dehydrogenase activity / metanephric collecting duct development / prostaglandin H2 endoperoxidase reductase activity / regulation of urine volume / all-trans-retinol dehydrogenase (NADP+) activity / renal water homeostasis / epithelial cell maturation / daunorubicin metabolic process / doxorubicin metabolic process / retinal dehydrogenase activity / aldose reductase (NADPH) activity / retinoid metabolic process / cellular hyperosmotic salinity response / electron transfer activity / carbohydrate metabolic process / negative regulation of apoptotic process / extracellular space / extracellular exosome / nucleoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.7 Å | ||||||
Authors | Podjarny, A. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 2000 Title: The structure of human aldose reductase bound to the inhibitor IDD384. Authors: Calderone, V. / Chevrier, B. / Van Zandt, M. / Lamour, V. / Howard, E. / Poterszman, A. / Barth, P. / Mitschler, A. / Lu, J. / Dvornik, D.M. / Klebe, G. / Kraemer, O. / Moorman, A.R. / Moras, D. / Podjarny, A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1el3.cif.gz | 82.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1el3.ent.gz | 61.6 KB | Display | PDB format |
PDBx/mmJSON format | 1el3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/el/1el3 ftp://data.pdbj.org/pub/pdb/validation_reports/el/1el3 | HTTPS FTP |
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-Related 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: 35898.340 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Organ: PLACENTA / Plasmid: PET15B / Production host: Escherichia coli (E. coli) / References: UniProt: P15121, aldose reductase |
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#2: Chemical | ChemComp-NAP / |
#3: Chemical | ChemComp-I84 / [ |
#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: 2.22 Å3/Da / Density % sol: 44.69 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 5 Details: 15 MG/ML AR, 5% PEG 6000, 50 MM AMMONIUM CITRATE PH 5.0 (DROP), 20% PEG 6000, 120 MM AMMONIUM CITRATE PH 5.0 (RESERVOIR), VAPOR DIFFUSION, HANGING DROP, temperature 277.0K | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 277 K | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 273 K |
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Diffraction source | Source: ROTATING ANODE / Type: SIEMENS / Wavelength: 1.5418 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jan 9, 1998 / Details: MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→14 Å / Num. all: 34934 / Num. obs: 33072 / % possible obs: 95.5 % / Observed criterion σ(F): 6 / Observed criterion σ(I): 3 / Redundancy: 1.5 % / Biso Wilson estimate: 13.6 Å2 / Rmerge(I) obs: 0.047 / Rsym value: 0.047 / Net I/σ(I): 12 |
Reflection shell | Resolution: 1.7→1.76 Å / Redundancy: 1.4 % / Rmerge(I) obs: 0.17 / Mean I/σ(I) obs: 5.4 / Rsym value: 0.17 / % possible all: 80 |
Reflection shell | *PLUS % possible obs: 80 % / Rmerge(I) obs: 0.17 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: ALDOSE REDUCTASE NATIVE Resolution: 1.7→8 Å / Rfactor Rfree error: 0.003 / Data cutoff high absF: 10466377.08 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 2 / σ(I): 1 / Stereochemistry target values: ENGH & HUBER
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 57.9872 Å2 / ksol: 0.447694 e/Å3 | ||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 16.8 Å2 | ||||||||||||||||||||||||||||||||||||||||
Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.7→8 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.7→1.76 Å / Rfactor Rfree error: 0.012 / Total num. of bins used: 8
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Xplor file |
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Software | *PLUS Name: X-PLOR / Version: 3.851 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 1.7 Å / Lowest resolution: 8 Å / σ(F): 2 / % reflection Rfree: 10 % | ||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 16.8 Å2 | ||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.225 / % reflection Rfree: 9.4 % / Rfactor Rwork: 0.214 / Rfactor obs: 0.214 |