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Yorodumi- PDB-2inz: Crystal Structure of Aldose Reductase complexed with 2-Hydroxyphe... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2inz | ||||||
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Title | Crystal Structure of Aldose Reductase complexed with 2-Hydroxyphenylacetic Acid | ||||||
Components | Aldose reductase | ||||||
Keywords | OXIDOREDUCTASE / TIM-Barrel / ARI / aldo-keto reductase | ||||||
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 / FOURIER SYNTHESIS / Resolution: 1.95 Å | ||||||
Authors | Harrison, D.H.T. / Pape, E. / Carlson, E. / Brownlee, J.M. | ||||||
Citation | Journal: Bioorg.Chem. / Year: 2006 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2inz.cif.gz | 79.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2inz.ent.gz | 59.1 KB | Display | PDB format |
PDBx/mmJSON format | 2inz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/in/2inz ftp://data.pdbj.org/pub/pdb/validation_reports/in/2inz | HTTPS FTP |
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-Related structure data
Related structure data | 2ineC 2ipwC 2iq0C 2iqdC 2is7C 2isfC 1az1S C: citing same article (ref.) S: Starting model for refinement |
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Similar 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: 35767.145 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: AKR1B1, ALDR1 / Plasmid: pET / Production host: Escherichia coli (E. coli) / Strain (production host): BL32(DE3) / References: UniProt: P15121, aldose reductase |
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#2: Chemical | ChemComp-NAP / |
#3: Chemical | ChemComp-OHP / ( |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 4 |
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-Sample preparation
Crystal | Density Matthews: 2.15 Å3/Da / Density % sol: 42.9 % |
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Crystal grow | Temperature: 277 K / pH: 5 Details: 20 % PEG 6000, 50 mM Citrate, subsequent glutaraldehyde x-link, ligand soak, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K, pH 5.00 |
-Data collection
Diffraction |
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Diffraction source |
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Detector |
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Radiation |
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Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 | ||||||||||||||||||||||||||||||
Reflection | Resolution: 1.95→30 Å / Num. obs: 23020 / % possible obs: 99 % / Observed criterion σ(I): 0 / Redundancy: 9.02 % / Rmerge(I) obs: 0.081 / Net I/σ(I): 28 | ||||||||||||||||||||||||||||||
Reflection shell | Resolution: 1.95→2 Å / Redundancy: 6.6 % / Rmerge(I) obs: 0.153 / Mean I/σ(I) obs: 24 / % possible all: 97.1 |
-Processing
Software |
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Refinement | Method to determine structure: FOURIER SYNTHESIS Starting model: PDB ENTRY 1AZ1 Resolution: 1.95→30 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 9.59 Å2 | ||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.95→30 Å
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LS refinement shell | Resolution: 1.95→2.04 Å / Total num. of bins used: 8
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