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Yorodumi- PDB-1t02: Crystal structure of a Statin bound to class II HMG-CoA reductase -
+Open data
-Basic information
Entry | Database: PDB / ID: 1t02 | ||||||
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Title | Crystal structure of a Statin bound to class II HMG-CoA reductase | ||||||
Components | 3-hydroxy-3-methylglutaryl-coenzyme A reductase | ||||||
Keywords | OXIDOREDUCTASE / Statin / HMG-CoA reductase / complex | ||||||
Function / homology | Function and homology information hydroxymethylglutaryl-CoA reductase (NADH) activity / hydroxymethylglutaryl-CoA reductase / hydroxymethylglutaryl-CoA reductase (NADPH) activity / ergosterol biosynthetic process / coenzyme A metabolic process / isoprenoid biosynthetic process / peroxisomal membrane Similarity search - Function | ||||||
Biological species | Pseudomonas mevalonii (bacteria) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.6 Å | ||||||
Authors | Tabernero, L. / Rodwell, V.W. / Stauffacher, C. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2003 Title: Crystal structure of a statin bound to a class II hydroxymethylglutaryl-CoA reductase. Authors: Tabernero, L. / Rodwell, V.W. / Stauffacher, C.V. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1t02.cif.gz | 151.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1t02.ent.gz | 118.3 KB | Display | PDB format |
PDBx/mmJSON format | 1t02.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1t02_validation.pdf.gz | 478.6 KB | Display | wwPDB validaton report |
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Full document | 1t02_full_validation.pdf.gz | 494.5 KB | Display | |
Data in XML | 1t02_validation.xml.gz | 17.7 KB | Display | |
Data in CIF | 1t02_validation.cif.gz | 26.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/t0/1t02 ftp://data.pdbj.org/pub/pdb/validation_reports/t0/1t02 | HTTPS FTP |
-Related structure data
Related structure data | 1qaxS 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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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 45641.242 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pseudomonas mevalonii (bacteria) / Gene: MVAA / Plasmid: pKK177-3 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) References: UniProt: P13702, hydroxymethylglutaryl-CoA reductase #2: Chemical | ChemComp-LVA / ( | #3: Chemical | ChemComp-SO4 / | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.72 Å3/Da / Density % sol: 54.81 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7 Details: pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 |
Detector | Type: RIGAKU RAXIS II / Detector: IMAGE PLATE |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→25 Å / Num. obs: 26296 / % possible obs: 87 % / Observed criterion σ(F): 2 / Redundancy: 4 % / Rsym value: 0.078 / Net I/σ(I): 15 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1qax Resolution: 2.6→15 Å / σ(F): 2 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 21.88 Å2 | ||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.6→15 Å
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Refine LS restraints |
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