+Open data
-Basic information
Entry | Database: PDB / ID: 2qmz | ||||||
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Title | Quinone Reductase 2 in Complex with Dopamine | ||||||
Components | Ribosyldihydronicotinamide dehydrogenase | ||||||
Keywords | OXIDOREDUCTASE / Quinone Reductase 2 / dopamine / dopamine oxidation / Parkinson's Disease / Cytoplasm / FAD / Flavoprotein / Metal-binding / Polymorphism / Zinc | ||||||
Function / homology | Function and homology information ribosyldihydronicotinamide dehydrogenase (quinone) / dihydronicotinamide riboside quinone reductase activity / quinone catabolic process / resveratrol binding / oxidoreductase activity, acting on other nitrogenous compounds as donors / melatonin binding / NAD(P)H dehydrogenase (quinone) activity / Phase I - Functionalization of compounds / chloride ion binding / FAD binding ...ribosyldihydronicotinamide dehydrogenase (quinone) / dihydronicotinamide riboside quinone reductase activity / quinone catabolic process / resveratrol binding / oxidoreductase activity, acting on other nitrogenous compounds as donors / melatonin binding / NAD(P)H dehydrogenase (quinone) activity / Phase I - Functionalization of compounds / chloride ion binding / FAD binding / electron transfer activity / oxidoreductase activity / protein homodimerization activity / extracellular exosome / zinc ion binding / nucleoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.1 Å | ||||||
Authors | Fu, Y. / Buryanovskyy, L. / Zhang, Z. | ||||||
Citation | Journal: To be Published Title: Quinone Reductase 2 Regulates Catecholamine Oxidation Authors: Fu, Y. / Buryanovskyy, L. / Zhang, Z. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2qmz.cif.gz | 114.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2qmz.ent.gz | 87.8 KB | Display | PDB format |
PDBx/mmJSON format | 2qmz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qm/2qmz ftp://data.pdbj.org/pub/pdb/validation_reports/qm/2qmz | 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: 25849.338 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: NQO2, NMOR2 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: P16083, EC: 1.10.99.2 #2: Chemical | #3: Chemical | #4: Chemical | #5: 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: 2.43 Å3/Da / Density % sol: 49.34 % |
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Crystal grow | Temperature: 300 K / Method: vapor diffusion, hanging drop / pH: 7 Details: Ammonium Sulfate (1.2-2 M), pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 300K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 19-BM / Wavelength: 1 Å |
Detector | Type: CUSTOM-MADE / Detector: CCD / Date: Jul 29, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→50 Å / Num. all: 30088 / Num. obs: 28148 / % possible obs: 93.6 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 / Redundancy: 6.7 % / Rmerge(I) obs: 0.101 / Net I/σ(I): 15 |
-Phasing
Phasing | Method: molecular replacement | ||||||||||||||||||
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Phasing MR | Cor.coef. Fo:Fc: 0.766 / Packing: 0.608
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.1→50 Å / FOM work R set: 0.849 / σ(F): 0
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Solvent computation | Bsol: 54.634 Å2 | ||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 23.337 Å2
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Refinement step | Cycle: LAST / Resolution: 2.1→50 Å
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Refine LS restraints |
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Xplor file |
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