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Yorodumi- PDB-1us0: Human Aldose Reductase in complex with NADP+ and the inhibitor ID... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1us0 | ||||||
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Title | Human Aldose Reductase in complex with NADP+ and the inhibitor IDD594 at 0.66 Angstrom | ||||||
Components | ALDOSE REDUCTASE | ||||||
Keywords | OXIDOREDUCTASE / NADP / IDD594 | ||||||
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 / SYNCHROTRON / MAD / Resolution: 0.66 Å | ||||||
Authors | Howard, E.I. / Sanishvili, R. / Cachau, R.E. / Mitschler, A. / Chevrier, B. / Barth, P. / Lamour, V. / Van Zandt, M. / Sibley, E. / Bon, C. ...Howard, E.I. / Sanishvili, R. / Cachau, R.E. / Mitschler, A. / Chevrier, B. / Barth, P. / Lamour, V. / Van Zandt, M. / Sibley, E. / Bon, C. / Moras, D. / Schneider, T.R. / Joachimiak, A. / Podjarny, A. | ||||||
Citation | Journal: Proteins / Year: 2004 Title: Ultrahigh Resolution Drug Design I: Details of Interactions in Human Aldose Reductase-Inhibitor Complex at 0.66 A. Authors: Howard, E.I. / Sanishvili, R. / Cachau, R.E. / Mitschler, A. / Chevrier, B. / Barth, P. / Lamour, V. / Van Zandt, M. / Sibley, E. / Bon, C. / Moras, D. / Schneider, T.R. / Joachimiak, A. / Podjarny, A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1us0.cif.gz | 182.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1us0.ent.gz | 151.7 KB | Display | PDB format |
PDBx/mmJSON format | 1us0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/us/1us0 ftp://data.pdbj.org/pub/pdb/validation_reports/us/1us0 | HTTPS FTP |
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-Related structure data
Related structure data | |
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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: 35898.340 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P15121, aldose reductase | ||||||
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#2: Chemical | ChemComp-NDP / | ||||||
#3: Chemical | ChemComp-LDT / | ||||||
#4: Chemical | #5: Water | ChemComp-HOH / | Compound details | CATALYZES THE NADPH-DEPENDENT REDUCTION OF A WIDE RANGE OF CARBONYL-CONTAINING COMPOUNDS INTO ...CATALYZES THE NADPH-DEPENDENT REDUCTION OF A WIDE RANGE OF CARBONYL-CONTAINING | Sequence details | THE CONFLICT ANNOTATED IN THE SEQADV CARDS BELOW HAS HAS BEEN DESCRIBED IN J.BIOL.CHEM. 264:14775 ...THE CONFLICT ANNOTATED IN THE SEQADV CARDS BELOW HAS HAS BEEN DESCRIBED IN J.BIOL.CHEM. 264:14775 (1989). THE MEDLINE ID FOR THIS REFERENCE IS 89359274 AND THE PUBMED ID FOR THE SAME IS 2504709. | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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-Sample preparation
Crystal | Density Matthews: 2.16 Å3/Da / Density % sol: 43.01 % |
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Crystal grow | pH: 5 Details: AS DESCRIBED IN LAMOUR ET AL. (1999) ACTA CRYSTALL. SECTION D 55:721-723, pH 5.00 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.653 |
Detector | Type: ANL / Detector: CCD / Date: Apr 19, 1999 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 SAGITTAL HORIZONTAL FOCUSING Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.653 Å / Relative weight: 1 |
Reflection | Resolution: 0.66→20 Å / Num. obs: 511265 / % possible obs: 89.1 % / Redundancy: 2.3 % / Rmerge(I) obs: 0.029 / Net I/σ(I): 14.5 |
Reflection shell | Resolution: 0.66→0.68 Å / Redundancy: 2.3 % / Rmerge(I) obs: 0.279 / Mean I/σ(I) obs: 2.4 / % possible all: 75.4 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 0.66→20 Å / Num. parameters: 33158 / Num. restraintsaints: 46316 / Cross valid method: FREE R-VALUE / σ(F): 0 / Stereochemistry target values: ENGH AND HUBER
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Solvent computation | Solvent model: KRETSINGER | |||||||||||||||||||||||||||||||||
Refine analyze | Num. disordered residues: 199 / Occupancy sum hydrogen: 2445.24 / Occupancy sum non hydrogen: 3054.25 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 0.66→20 Å
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Refine LS restraints |
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