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Yorodumi- PDB-1dla: NOVEL NADPH-BINDING DOMAIN REVEALED BY THE CRYSTAL STRUCTURE OF A... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1dla | ||||||
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Title | NOVEL NADPH-BINDING DOMAIN REVEALED BY THE CRYSTAL STRUCTURE OF ALDOSE REDUCTASE | ||||||
Components | ALDOSE REDUCTASE | ||||||
Keywords | OXIDOREDUCTASE(NADP) | ||||||
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 / Resolution: 3 Å | ||||||
Authors | Rondeau, J.-M. / Tete-Favier, F. / Podjarny, A. / Reymann, J.-M. / Barth, P. / Biellmann, J.-F. / Moras, D. | ||||||
Citation | 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. #1: 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. #2: Journal: J.Mol.Biol. / Year: 1987 Title: Crystallization and Preliminary X-Ray Study of Pig Lens Aldose Reductase Authors: Rondeau, J.-M. / Samama, J.-P. / Samama, B. / Barth, P. / Moras, D. / Biellmann, J.-F. | ||||||
History |
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Remark 700 | SHEET THE SHEETS PRESENTED AS *BRA*, *BRB*, *BRC*, AND *BRD* ON SHEET RECORDS BELOW ARE ACTUALLY ...SHEET THE SHEETS PRESENTED AS *BRA*, *BRB*, *BRC*, AND *BRD* ON SHEET RECORDS BELOW ARE ACTUALLY EIGHT-STRANDED BETA-BARRELS. THESE ARE REPRESENTED BY NINE-STRANDED SHEETS IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1dla.cif.gz | 49 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1dla.ent.gz | 30.7 KB | Display | PDB format |
PDBx/mmJSON format | 1dla.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1dla_validation.pdf.gz | 353 KB | Display | wwPDB validaton report |
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Full document | 1dla_full_validation.pdf.gz | 353 KB | Display | |
Data in XML | 1dla_validation.xml.gz | 1.4 KB | Display | |
Data in CIF | 1dla_validation.cif.gz | 12.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/dl/1dla ftp://data.pdbj.org/pub/pdb/validation_reports/dl/1dla | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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3 |
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4 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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-Components
#1: Protein | Mass: 35710.926 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Sus scrofa (pig) / References: UniProt: P80276, aldose reductase Sequence details | SEQUENCE ADVISORY NOTICE: SEQUENCE NOT IN SWISS-PROT DATA BASE. THE SEQUENCE PRESENTED BELOW IS ...SEQUENCE ADVISORY NOTICE: SEQUENCE NOT IN SWISS-PROT DATA BASE. THE SEQUENCE PRESENTED BELOW IS THAT DESCRIBED BY M. JAQUINOD ET AL.,( EUR. J. BIOCHEM. 218, 893, 1993). | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.6 Å3/Da / Density % sol: 52.69 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 4 ℃ / pH: 6.2 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 82 Å / Num. obs: 40833 / % possible obs: 82 % / Num. measured all: 128597 / Rmerge(I) obs: 0.065 |
-Processing
Software |
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Refinement | Rfactor Rwork: 0.219 / Rfactor obs: 0.219 / Highest resolution: 3 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 3 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.219 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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