[English] 日本語
![](img/lk-miru.gif)
- PDB-4bvr: Cyanuric acid hydrolase: evolutionary innovation by structural co... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 4bvr | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
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 |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 147.4 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 114.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 461.8 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 465.1 KB | Display | |
Data in XML | ![]() | 25.8 KB | Display | |
Data in CIF | ![]() | 35.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4bvqC ![]() 4bvsC ![]() 4bvtC ![]() 3zgr C: citing same article ( S: Starting model for refinement |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||||||||||||
Unit cell |
| ||||||||||||||||||
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
|
-
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 / | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.79 Å3/Da / Density % sol: 55.9 % / Description: NONE |
---|---|
Crystal grow | pH: 6.6 Details: THE PROTEIN WAS AT 1 MG/ML AFTER DIALYSIS WITH HEPES BUFFER AND CYANURIC ACID, THIS WAS ADDED IN A 3:1 RATIO TO THE RESERVIOR SOLUTION OF 38% V/V PEG 400 AND 100 MM HEPES PH 6.6 |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Nov 16, 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: 2.58→42.5 Å / Num. obs: 23460 / % possible obs: 100 % / Observed criterion σ(I): 1 / Redundancy: 11.1 % / Rmerge(I) obs: 0.14 / Net I/σ(I): 12.5 |
Reflection shell | Resolution: 2.58→2.72 Å / Redundancy: 11.3 % / Rmerge(I) obs: 0.8 / Mean I/σ(I) obs: 3.1 / % possible all: 100 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 3ZGR ![]() 3zgr Resolution: 2.58→41.59 Å / Cor.coef. Fo:Fc: 0.954 / Cor.coef. Fo:Fc free: 0.926 / SU B: 9.468 / SU ML: 0.206 / Cross valid method: THROUGHOUT / ESU R: 1.497 / ESU R Free: 0.291 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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: 50.042 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.58→41.59 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
|