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- PDB-2gvc: Crystal structure of flavin-containing monooxygenase (FMO)from S.... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2gvc | ||||||
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Title | Crystal structure of flavin-containing monooxygenase (FMO)from S.pombe and substrate (methimazole) complex | ||||||
![]() | monooxygenase | ||||||
![]() | OXIDOREDUCTASE / FMO / FAD / methimazole / oxygenase / PSI / Structural Genomics / Protein Structure Initiative / New York SGX Research Center for Structural Genomics / NYSGXRC | ||||||
Function / homology | ![]() Oxidoreductases; Acting on paired donors, with incorporation or reduction of molecular oxygen; With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor / N,N-dimethylaniline monooxygenase activity / cellular detoxification / FAD binding / NADP binding / endoplasmic reticulum membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Eswaramoorthy, S. / Swaminathan, S. / Burley, S.K. / New York SGX Research Center for Structural Genomics (NYSGXRC) | ||||||
![]() | ![]() Title: Mechanism of action of a flavin-containing monooxygenase. Authors: Eswaramoorthy, S. / Bonanno, J.B. / Burley, S.K. / Swaminathan, S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 368.2 KB | Display | ![]() |
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PDB format | ![]() | 299.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.5 MB | Display | ![]() |
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Full document | ![]() | 1.5 MB | Display | |
Data in XML | ![]() | 74.8 KB | Display | |
Data in CIF | ![]() | 99.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1vqwSC ![]() 2gv8C S: Starting model for refinement C: citing same article ( |
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Similar structure data | |
Other databases |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Components
-Protein , 1 types, 4 molecules ABDE
#1: Protein | Mass: 50179.543 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Production host: ![]() ![]() |
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-Non-polymers , 5 types, 553 molecules ![](data/chem/img/PEO.gif)
![](data/chem/img/FAD.gif)
![](data/chem/img/MMZ.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/FAD.gif)
![](data/chem/img/MMZ.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-PEO / #3: Chemical | ChemComp-FAD / #4: Chemical | ChemComp-MMZ / #5: Chemical | ChemComp-GOL / #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.15 Å3/Da / Density % sol: 60.97 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 5.6 Details: PEG 3350, Ammonium Acetate, pH 5.6, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Jul 12, 2005 |
Radiation | Monochromator: Si 111 CHANNEL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.1 Å / Relative weight: 1 |
Reflection | Resolution: 2.22→50 Å / Num. all: 112153 / Num. obs: 112153 / % possible obs: 92.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.3 % / Rmerge(I) obs: 0.067 / Net I/σ(I): 9.3 |
Reflection shell | Resolution: 2.22→2.3 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.321 / Num. unique all: 9155 / % possible all: 75.7 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: pdb entry 1VQW Resolution: 2.22→50 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber Details: The side chain atoms of GLU 444 were not modeled due to lack of electron density.
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Refinement step | Cycle: LAST / Resolution: 2.22→50 Å
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Refine LS restraints |
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