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- PDB-4bvt: Cyanuric acid hydrolase: evolutionary innovation by structural co... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4bvt | |||||||||
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Title | Cyanuric acid hydrolase: evolutionary innovation by structural concatenation | |||||||||
![]() | CYANURIC ACID AMIDOHYDROLASE | |||||||||
![]() | HYDROLASE / AMIDASE | |||||||||
Function / homology | ![]() cyanuric acid amidohydrolase / cyanuric acid amidohydrolase activity / atrazine catabolic process / metal ion binding Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Peat, T.S. / Balotra, S. / Wilding, M. / French, N.G. / Briggs, L.J. / Panjikar, S. / Cowieson, N. / Newman, J. / Scott, C. | |||||||||
![]() | ![]() Title: Cyanuric Acid Hydrolase: Evolutionary Innovation by Structural Concatenation. Authors: Peat, T.S. / Balotra, S. / Wilding, M. / French, N.G. / Briggs, L.J. / Panjikar, S. / Cowieson, N. / Newman, J. / Scott, C. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 146.8 KB | Display | ![]() |
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PDB format | ![]() | 114.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 463.5 KB | Display | ![]() |
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Full document | ![]() | 468.6 KB | Display | |
Data in XML | ![]() | 26.2 KB | Display | |
Data in CIF | ![]() | 35.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4bvqC ![]() 4bvrC ![]() 4bvsC ![]() 3zgr C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: _ / Ens-ID: 1 / Beg auth comp-ID: HIS / Beg label comp-ID: HIS / End auth comp-ID: ALA / End label comp-ID: ALA / Refine code: _ / Auth seq-ID: 0 - 363 / Label seq-ID: 20 - 383
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Components
#1: Protein | Mass: 40418.656 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Description: GENE SYNTHESIZED BASED ON SEQUENCE FROM ACCESSION NO U66917 Production host: ![]() ![]() #2: Chemical | #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.79 Å3/Da / Density % sol: 55.9 % / Description: NONE |
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Crystal grow | pH: 7 Details: THE PROTEIN WAS DIALYSED AGAINST HEPES BUFFER WITH BARBITURIC ACID, THE FINAL CONCENTRATION OF PROTEIN WAS 2 MG/ML AND THIS WAS SET UP IN A 1:1 RATIO AGAINST 180 MM NACL, 31% V/V PEG 400 AND 100 MM HEPES PH 7.0. |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Oct 18, 2012 / Details: MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9537 Å / Relative weight: 1 |
Reflection | Resolution: 3.09→43.1 Å / Num. obs: 13929 / % possible obs: 99.5 % / Observed criterion σ(I): 1 / Redundancy: 9.7 % / Rmerge(I) obs: 0.14 / Net I/σ(I): 12.9 |
Reflection shell | Resolution: 3.09→3.26 Å / Redundancy: 9.2 % / Rmerge(I) obs: 0.62 / Mean I/σ(I) obs: 3.6 / % possible all: 96.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 3ZGR ![]() 3zgr Resolution: 3.1→43.18 Å / Cor.coef. Fo:Fc: 0.952 / Cor.coef. Fo:Fc free: 0.92 / SU B: 17.921 / SU ML: 0.302 / Cross valid method: THROUGHOUT / ESU R Free: 0.422 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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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: 63.99 Å2
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Refinement step | Cycle: LAST / Resolution: 3.1→43.18 Å
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Refine LS restraints |
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