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- PDB-6vl7: Crystal structure of the H583C mutant of GoxA soaked with glycine -
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Open data
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Basic information
Entry | Database: PDB / ID: 6vl7 | ||||||
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Title | Crystal structure of the H583C mutant of GoxA soaked with glycine | ||||||
![]() | Glycine oxidase | ||||||
![]() | OXIDOREDUCTASE / CTQ | ||||||
Function / homology | L-Lysine epsilon oxidase, N-terminal / L-lysine epsilon oxidase, C-terminal / L-Lysine epsilon oxidase N-terminal / L-lysine epsilon oxidase C-terminal domain / metal ion binding / DI(HYDROXYETHYL)ETHER / TRIETHYLENE GLYCOL / Uncharacterized protein![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Yukl, E.T. | ||||||
![]() | ![]() Title: Roles of active-site residues in catalysis, substrate binding, cooperativity, and the reaction mechanism of the quinoprotein glycine oxidase. Authors: Mamounis, K.J. / Yukl, E.T. / Davidson, V.L. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1.3 MB | Display | ![]() |
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PDB format | ![]() | 1.1 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 6vmfC ![]() 6vmvC ![]() 6vmwC ![]() 6bywS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
-Protein , 1 types, 4 molecules ABCD
#1: Protein | Mass: 91491.781 Da / Num. of mol.: 4 / Mutation: H583C Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: N475_19905 / Production host: ![]() ![]() |
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-Non-polymers , 5 types, 1562 molecules ![](data/chem/img/MG.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/PEG.gif)
![](data/chem/img/PGE.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/PEG.gif)
![](data/chem/img/PGE.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-MG / #3: Chemical | ChemComp-SO4 / #4: Chemical | ChemComp-PEG / | #5: Chemical | #6: Water | ChemComp-HOH / | |
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-Details
Has ligand of interest | N |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.63 Å3/Da / Density % sol: 53.21 % |
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Crystal grow | Temperature: 293 K / Method: batch mode / pH: 7.5 Details: 1uL protein was combined with 1uL precipitant solution containing 25% PEG 3350, 0.1 M HEPES pH 7.5 and 0.1 M ammonium sulfate |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jun 30, 2018 |
Radiation | Monochromator: Double-crystal, Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.14→49.191 Å / Num. obs: 207973 / % possible obs: 99.4 % / Redundancy: 3.7 % / CC1/2: 0.997 / Rmerge(I) obs: 0.087 / Rpim(I) all: 0.051 / Rrim(I) all: 0.101 / Net I/σ(I): 9.2 |
Reflection shell | Resolution: 2.14→2.18 Å / Redundancy: 3.9 % / Rmerge(I) obs: 0.605 / Mean I/σ(I) obs: 2.1 / Num. unique obs: 10307 / CC1/2: 0.783 / Rpim(I) all: 0.354 / Rrim(I) all: 0.703 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 6BYW Resolution: 2.14→49.191 Å / SU ML: 0.22 / Cross valid method: THROUGHOUT / σ(F): 1.33 / Phase error: 23.73
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 162.47 Å2 / Biso mean: 47.6067 Å2 / Biso min: 18.09 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.14→49.191 Å
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0
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Refinement TLS params. | Method: refined / Origin x: 16.1741 Å / Origin y: -142.5305 Å / Origin z: 233.4471 Å
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Refinement TLS group |
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