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- PDB-2ipw: Crystal Structure of C298A W219Y Aldose Reductase complexed with ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2ipw | ||||||
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Title | Crystal Structure of C298A W219Y Aldose Reductase complexed with Dichlorophenylacetic acid | ||||||
![]() | Aldose reductase | ||||||
![]() | OXIDOREDUCTASE / TIM-Barrel / ARI / aldo-keto reductase | ||||||
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 | ![]() ![]() | ||||||
![]() | Harrison, D.H.T. / Pape, E. / Brownlee, J.M. | ||||||
![]() | ![]() Title: Structural and thermodynamic studies of simple aldose reductase-inhibitor complexes. Authors: Brownlee, J.M. / Carlson, E. / Milne, A.C. / Pape, E. / Harrison, D.H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 78.2 KB | Display | ![]() |
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PDB format | ![]() | 57.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 723.4 KB | Display | ![]() |
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Full document | ![]() | 727.3 KB | Display | |
Data in XML | ![]() | 14.3 KB | Display | |
Data in CIF | ![]() | 19.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2ineC ![]() 2inzC ![]() 2iq0C ![]() 2iqdC ![]() 2is7C ![]() 2isfC ![]() 1az1S C: citing same article ( S: Starting model for refinement |
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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: 35712.047 Da / Num. of mol.: 1 / Mutation: W219Y, C298A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-NAP / |
#3: Chemical | ChemComp-2CL / ( |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.14 Å3/Da / Density % sol: 42.6 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 5 Details: 20 % PEG 6000, 50 mM Citrate, subsequent glutaraldehyde x-link, ligand soak, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
Diffraction |
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Diffraction source | Source: ![]() | |||||||||||||||
Detector |
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Radiation | Monochromator: graphite / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 | |||||||||||||||
Reflection | Resolution: 2→30 Å / Num. all: 21429 / Num. obs: 20062 / % possible obs: 93.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.3 % / Rmerge(I) obs: 0.103 / Χ2: 3.138 / Net I/σ(I): 13.2 | |||||||||||||||
Reflection shell | Resolution: 2→2.03 Å / Redundancy: 1.9 % / Rmerge(I) obs: 0.086 / Mean I/σ(I) obs: 10.3 / Num. unique all: 724 / Χ2: 1.24 / % possible all: 70.7 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1AZ1 Resolution: 2→30 Å / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 17.817 Å2 | ||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→30 Å
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LS refinement shell | Resolution: 2→2.1 Å
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