+Open data
-Basic information
Entry | Database: PDB / ID: 1cyd | ||||||
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Title | CARBONYL REDUCTASE COMPLEXED WITH NADPH AND 2-PROPANOL | ||||||
Components | CARBONYL REDUCTASE | ||||||
Keywords | OXIDOREDUCTASE / SHORT-CHAIN DEHYDROGENASE | ||||||
Function / homology | Function and homology information L-xylulose reductase (NADPH) activity / xylulose metabolic process / carbonyl reductase (NADPH) / carbonyl reductase (NADPH) activity / : / NADH oxidation / glucose metabolic process / mitochondrial matrix / mitochondrion / identical protein binding Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.8 Å | ||||||
Authors | Tanaka, N. / Nonaka, T. / Mitsui, Y. | ||||||
Citation | Journal: Structure / Year: 1996 Title: Crystal structure of the ternary complex of mouse lung carbonyl reductase at 1.8 A resolution: the structural origin of coenzyme specificity in the short-chain dehydrogenase/reductase family. Authors: Tanaka, N. / Nonaka, T. / Nakanishi, M. / Deyashiki, Y. / Hara, A. / Mitsui, Y. #1: Journal: To be Published Title: Crystallization of Mouse Lung Carbonyl Reductase Complexed with Nadph and Analysis of Symmetry of its Tetrameric Molecule Authors: Tanaka, N. / Nonaka, T. / Nakanishi, M. / Deyashiki, Y. / Hara, A. / Mitsui, Y. #2: Journal: Eur.J.Biochem. / Year: 1995 Title: Cloning, Expression and Tissue Distribution of Mouse Tetrameric Carbonyl Reductase. Identity with an Adipocyte 27-kDa Protein Authors: Nakanishi, M. / Deyashiki, Y. / Ohshima, K. / Hara, A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1cyd.cif.gz | 200.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1cyd.ent.gz | 162.1 KB | Display | PDB format |
PDBx/mmJSON format | 1cyd.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1cyd_validation.pdf.gz | 692.8 KB | Display | wwPDB validaton report |
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Full document | 1cyd_full_validation.pdf.gz | 708.8 KB | Display | |
Data in XML | 1cyd_validation.xml.gz | 22.3 KB | Display | |
Data in CIF | 1cyd_validation.cif.gz | 34.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cy/1cyd ftp://data.pdbj.org/pub/pdb/validation_reports/cy/1cyd | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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-Components
#1: Protein | Mass: 25989.178 Da / Num. of mol.: 4 / Source method: isolated from a natural source Details: THIS PROTEIN IS IDENTICAL WITH AN ADIPOCYTE 27-KDA PROTEIN Source: (natural) Mus musculus (house mouse) / Cell: EPITHELIAL CELL / Organ: LUNG / Organelle: MITOCHONDRION / Strain: DDY MICE / Tissue: EPITHELIAL / References: UniProt: P08074, carbonyl reductase (NADPH) #2: Chemical | ChemComp-NDP / #3: Chemical | ChemComp-IPA / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.46 Å3/Da / Density % sol: 47 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.5 / Details: pH 7.5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 277 K |
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Diffraction source | Source: SYNCHROTRON / Site: Photon Factory / Beamline: BL-6A / Wavelength: 1 |
Detector | Type: WEISSENBERG / Detector: DIFFRACTOMETER / Date: Mar 3, 1994 / Details: BENT MIRROR |
Radiation | Monochromator: SI(111) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→79.1 Å / Num. obs: 67478 / % possible obs: 72.4 % / Observed criterion σ(I): 1 / Redundancy: 3.3 % / Rmerge(I) obs: 0.063 |
Reflection | *PLUS Lowest resolution: 79 Å / Num. measured all: 224849 |
Reflection shell | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 2 Å / % possible obs: 49.7 % |
-Processing
Software |
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Refinement | Resolution: 1.8→10 Å / σ(F): 1
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Displacement parameters | Biso mean: 14.09 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.15 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→10 Å
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Refine LS restraints |
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