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- PDB-2i16: 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: 2i16 | ||||||
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Title | Human aldose reductase in complex with NADP+ and the inhibitor IDD594 at temperature of 15K | ||||||
![]() | Aldose reductase | ||||||
![]() | OXIDOREDUCTASE / NADP / IDD594 | ||||||
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. / Mitshler, A. / Hasemann, I. / Schneider, T. / Cousido, A. / Lunin, V.Y. / Joachimiak, A. / Podjarny, A. | ||||||
![]() | ![]() Title: Ultrahigh-resolution study of protein atomic displacement parameters at cryotemperatures obtained with a helium cryostat. Authors: Petrova, T. / Ginell, S. / Mitschler, A. / Hazemann, I. / Schneider, T. / Cousido, A. / Lunin, V.Y. / Joachimiak, 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 | ![]() | 224.9 KB | Display | ![]() |
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PDB format | ![]() | 215 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 966.7 KB | Display | ![]() |
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Full document | ![]() | 974.4 KB | Display | |
Data in XML | ![]() | 21.7 KB | Display | |
Data in CIF | ![]() | 35.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2i17C ![]() 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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Details | The biological assembly is a monomer |
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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 | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.16 Å3/Da / Density % sol: 42.97 % Description: DATA WERE COLLECTED AT 15K USING COLD HELIUM STREAM FOR COOLING. |
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Crystal grow | pH: 5 / Details: pH 5.0 |
-Data collection
Diffraction | Mean temperature: 15 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD 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: 0.635 Å / Relative weight: 1 |
Reflection | Resolution: 0.81→50 Å / Num. all: 295088 / Num. obs: 263010 / % possible obs: 95.8 % / Observed criterion σ(F): 4 / Biso Wilson estimate: 3 Å2 / Rmerge(I) obs: 0.053 / Net I/σ(I): 15.2 |
Reflection shell | Resolution: 0.81→0.84 Å / Rmerge(I) obs: 0.204 / Mean I/σ(I) obs: 5.1 / % possible all: 93.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: pdb entry 1US0 Resolution: 0.81→50 Å / Num. parameters: 34437 / Num. restraintsaints: 25444 / Cross valid method: FREE R / σ(F): 0 / Stereochemistry target values: ENGH AND HUBER Details: RESIDUES IN SINGLE CONFORMATION WERE REFINED WITHOUT RESTRAINTS
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Refine analyze | Num. disordered residues: 279 / Occupancy sum hydrogen: 2397.91 / Occupancy sum non hydrogen: 3022.55 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 0.81→50 Å
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Refine LS restraints |
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