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- PDB-8cp5: Structure of Aspartate-N-hydroxylase (FzmM)from Streptomyces sp. ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 8cp5 | ||||||
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Title | Structure of Aspartate-N-hydroxylase (FzmM)from Streptomyces sp. V2: complex with NADPH and Sulphate | ||||||
![]() | FAD-binding protein | ||||||
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Function / homology | FAD-dependent urate hydroxylase HpyO, FAD/NAD(P)-binding domain / FAD-NAD(P)-binding / FAD/NAD(P)-binding domain superfamily / ![]() ![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Rotilio, L. / Mattevi, A. | ||||||
Funding support | ![]()
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![]() | ![]() Title: A biosynthetic aspartate N-hydroxylase performs successive oxidations by holding intermediates at a site away from the catalytic center. Authors: Rotilio, L. / Boverio, A. / Nguyen, Q.T. / Mannucci, B. / Fraaije, M.W. / Mattevi, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 240.1 KB | Display | ![]() |
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PDB format | ![]() | 197.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 8cp2C C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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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, 2 molecules AB
#1: Protein | Mass: 65830.266 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Non-polymers , 6 types, 88 molecules ![](data/chem/img/FAD.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/NAP.gif)
![](data/chem/img/PEG.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/NAP.gif)
![](data/chem/img/PEG.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ![]() #3: Chemical | ChemComp-SO4 / ![]() #4: Chemical | ChemComp-GOL / | ![]() #5: Chemical | ![]() #6: Chemical | ![]() #7: Water | ChemComp-HOH / | ![]() |
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-Details
Has ligand of interest | Y |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal grow![]() | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7 / Details: 0.1 M Hepes pH 7 1.6 M Ammonium sulphate |
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-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS EIGER X 4M / Detector: PIXEL / Date: Jul 9, 2022 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2.54→80.98 Å / Num. obs: 91662 / % possible obs: 99.1 % / Redundancy: 10.8 % / CC1/2: 0.996 / Rmerge(I) obs: 0.194 / Rpim(I) all: 0.061 / Rrim(I) all: 0.203 / Χ2: 0.99 / Net I/σ(I): 10.1 / Num. measured all: 993652 |
Reflection shell | Resolution: 2.54→2.58 Å / % possible obs: 86.4 % / Redundancy: 10.3 % / Rmerge(I) obs: 1.8 / Num. measured all: 40976 / Num. unique obs: 3985 / CC1/2: 0.293 / Rpim(I) all: 1.266 / Rrim(I) all: 4.151 / Χ2: 0.94 / Net I/σ(I) obs: 0.6 |
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Processing
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Refinement | Method to determine structure![]() ![]()
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 49.772 Å2
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Refinement step | Cycle: 1 / Resolution: 2.54→80.98 Å
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Refine LS restraints |
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