+Open data
-Basic information
Entry | Database: PDB / ID: 1ah4 | ||||||
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Title | PIG ALDOSE REDUCTASE, HOLO FORM | ||||||
Components | ALDOSE REDUCTASE | ||||||
Keywords | OXIDOREDUCTASE / ALDOSE REDUCTASE / INHIBITION / DIABETES | ||||||
Function / homology | Function and homology information glycerol dehydrogenase (NADP+) activity / D/L-glyceraldehyde reductase / aldose reductase / NADP-retinol dehydrogenase / allyl-alcohol dehydrogenase / allyl-alcohol dehydrogenase activity / prostaglandin H2 endoperoxidase reductase activity / all-trans-retinol dehydrogenase (NADP+) activity / retinal dehydrogenase activity / aldose reductase (NADPH) activity ...glycerol dehydrogenase (NADP+) activity / D/L-glyceraldehyde reductase / aldose reductase / NADP-retinol dehydrogenase / allyl-alcohol dehydrogenase / allyl-alcohol dehydrogenase activity / prostaglandin H2 endoperoxidase reductase activity / all-trans-retinol dehydrogenase (NADP+) activity / retinal dehydrogenase activity / aldose reductase (NADPH) activity / retinoid metabolic process / cytosol Similarity search - Function | ||||||
Biological species | Sus scrofa (pig) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å | ||||||
Authors | Moras, D. / Podjarny, A. | ||||||
Citation | Journal: Structure / Year: 1997 Title: A 'specificity' pocket inferred from the crystal structures of the complexes of aldose reductase with the pharmaceutically important inhibitors tolrestat and sorbinil. Authors: Urzhumtsev, A. / Tete-Favier, F. / Mitschler, A. / Barbanton, J. / Barth, P. / Urzhumtseva, L. / Biellmann, J.F. / Podjarny, A. / Moras, D. #1: Journal: Eur.J.Med.Chem. / Year: 1995 Title: Aldose Reductase from Pig Lens Authors: Tete-Favier, F. / Barth, P. / Mitschler, A. / Podjarny, A.D. / Rondeau, J.-M. / Urzhumtsev, A. / Biellemann, J.-F. / Moras, D. #2: Journal: Acta Crystallogr.,Sect.D / Year: 1993 Title: Structure Determination of Aldose Reductase: Joys and Traps of Local Symmetry Averaging Authors: Tete-Favier, F. / Rondeau, J.-M. / Podjarny, A. / Moras, D. #3: Journal: Nature / Year: 1992 Title: Novel Nadph-Binding Domain Revealed by the Crystal Structure of Aldose Reductase Authors: Rondeau, J.M. / Tete-Favier, F. / Podjarny, A. / Reymann, J.M. / Barth, P. / Biellmann, J.F. / Moras, D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ah4.cif.gz | 95.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ah4.ent.gz | 73.1 KB | Display | PDB format |
PDBx/mmJSON format | 1ah4.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1ah4_validation.pdf.gz | 717.5 KB | Display | wwPDB validaton report |
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Full document | 1ah4_full_validation.pdf.gz | 725.4 KB | Display | |
Data in XML | 1ah4_validation.xml.gz | 17.8 KB | Display | |
Data in CIF | 1ah4_validation.cif.gz | 25.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ah/1ah4 ftp://data.pdbj.org/pub/pdb/validation_reports/ah/1ah4 | HTTPS FTP |
-Related 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: 35824.035 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / Organ: EYE / Tissue: LENS / References: UniProt: P80276, aldose reductase |
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#2: Chemical | ChemComp-NAP / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.6 Å3/Da / Density % sol: 51 % | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 6.2 Details: 6 MG/ML AR, 2.5% PEG 6000,25 MM MESPH 6.2 (DROP),20% PEG 6000,25 MM MESPH 6.2 (RESERVOIR) | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 273 K |
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Diffraction source | Source: SYNCHROTRON / Site: LURE / Beamline: DW32 / Wavelength: 0.91 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Mar 1, 1996 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.91 Å / Relative weight: 1 |
Reflection | Resolution: 2→15 Å / Num. obs: 24329 / % possible obs: 97 % / Observed criterion σ(I): 3 / Redundancy: 3.4 % / Rsym value: 0.051 / Net I/σ(I): 28.5 |
Reflection shell | Resolution: 2→2.1 Å / Redundancy: 2.6 % / Mean I/σ(I) obs: 5.2 / Rsym value: 0.312 / % possible all: 93 |
Reflection | *PLUS Rmerge(I) obs: 0.051 |
Reflection shell | *PLUS % possible obs: 93 % |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: ALDOSE REDUCTASE, APO FORM Resolution: 2→6 Å / Data cutoff high absF: 10000000 / Data cutoff low absF: 0.001 / Isotropic thermal model: RESTRAINED / Cross valid method: A POSTERIORI / σ(F): 2
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Displacement parameters | Biso mean: 37.1 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→6 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2→2.1 Å / Total num. of bins used: 8
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Xplor file |
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