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- PDB-3ghs: Human aldose reductase in complex with NADP+ and the inhibitor ID... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3ghs | ||||||
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Title | Human aldose reductase in complex with NADP+ and the inhibitor IDD594. Investigation of global effects of radiation damage on protein structure. Second stage of radiation damage. | ||||||
![]() | Aldose reductase | ||||||
![]() | OXIDOREDUCTASE / Acetylation / Cataract / Cytoplasm / NADP / Phosphoprotein / Polymorphism | ||||||
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 | ![]() ![]() ![]() | ||||||
![]() | Petrova, T. / Ginell, S. / Hazemann, I. / Mitschler, A. / Podjarny, A. / Joachimiak, A. | ||||||
![]() | ![]() Title: X-ray-radiation-induced cooperative atomic movements in protein. Authors: Petrova, T. / Lunin, V.Y. / Ginell, S. / Hazemann, I. / Lazarski, K. / Mitschler, A. / Podjarny, A. / Joachimiak, 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 | ![]() | 195.9 KB | Display | ![]() |
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PDB format | ![]() | 155 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 992.6 KB | Display | ![]() |
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Full document | ![]() | 1001.6 KB | Display | |
Data in XML | ![]() | 23.8 KB | Display | |
Data in CIF | ![]() | 38 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3ghrC ![]() 3ghtC ![]() 3ghuC ![]() 1us0S S: Starting model for refinement C: citing same article ( |
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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: 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-NDP / |
#3: Chemical | ChemComp-LDT / |
#4: Chemical | ChemComp-CIT / |
#5: Water | ChemComp-HOH / |
Sequence details | AUTHORS STATE THAT RESIDUE NUMBER 4 IS ILE. ELECTRON DENSITY FOR THIS RESIDUE IS VERY CLEAR |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.17 Å3/Da / Density % sol: 43.41 % |
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Crystal grow | Temperature: 277 K / pH: 5 Details: The co-crystallization with IDD594 was carried out at room temperature (ratios protein/coenzyme/inhibitor = 1/2/2). pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM Q315r / Detector: CCD / Date: Aug 20, 2007 Details: 1.02-M FLAT MIRROR MADE OF ZERODUR PROVIDING VERTICAL FOCUSING AND REJECTION OF HARMONIC CONTAMINATION |
Radiation | Monochromator: DOUBLE CRYSTAL MONOCHROMATOR UTILIZING A SI-111 AND SAGITAL HORIZONTAL FOCUSING Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.91996 Å / Relative weight: 1 |
Reflection | Resolution: 0.98→50 Å / Num. obs: 164625 / % possible obs: 93.9 % / Observed criterion σ(I): 0 / Redundancy: 3.7 % / Rmerge(I) obs: 0.03 / Rsym value: 0.04 / Net I/σ(I): 28.9 |
Reflection shell | Resolution: 0.98→1.02 Å / Redundancy: 3 % / Rmerge(I) obs: 0.34 / Mean I/σ(I) obs: 2.33 / % possible all: 82.7 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1US0 Resolution: 1→50 Å / σ(F): 4 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1→50 Å
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