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- PDB-4cnx: Surface residue engineering of bovine carbonic anhydrase to an ex... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4cnx | ||||||
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Title | Surface residue engineering of bovine carbonic anhydrase to an extreme halophilic enzyme for potential application in postcombustion CO2 capture | ||||||
![]() | CARBONIC ANHYDRASE 2 | ||||||
![]() | LYASE / PROTEIN ENGINEERING / CO2 CAPTURE | ||||||
Function / homology | ![]() positive regulation of dipeptide transmembrane transport / regulation of monoatomic anion transport / cyanamide hydratase / cyanamide hydratase activity / angiotensin-activated signaling pathway / regulation of intracellular pH / carbonic anhydrase / carbonate dehydratase activity / carbon dioxide transport / one-carbon metabolic process ...positive regulation of dipeptide transmembrane transport / regulation of monoatomic anion transport / cyanamide hydratase / cyanamide hydratase activity / angiotensin-activated signaling pathway / regulation of intracellular pH / carbonic anhydrase / carbonate dehydratase activity / carbon dioxide transport / one-carbon metabolic process / apical part of cell / zinc ion binding / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Warden, A. / Newman, J. / Peat, T.S. / Seabrook, S. / Williams, M. / Dojchinov, G. / Haritos, V. | ||||||
![]() | ![]() Title: Rational Engineering of a Mesohalophilic Carbonic Anhydrase to an Extreme Halotolerant Biocatalyst. Authors: Warden, A.C. / Williams, M. / Peat, T.S. / Seabrook, S.A. / Newman, J. / Dojchinov, G. / Haritos, V.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 | ![]() | 142.3 KB | Display | ![]() |
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PDB format | ![]() | 109.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 437.5 KB | Display | ![]() |
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Full document | ![]() | 443 KB | Display | |
Data in XML | ![]() | 17 KB | Display | |
Data in CIF | ![]() | 26.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4cnrC ![]() 4cnvC ![]() 4cnwC ![]() 5a25C ![]() 3ml2S 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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Unit cell |
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Components
#1: Protein | Mass: 29426.455 Da / Num. of mol.: 1 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-ZN / |
#3: Chemical | ChemComp-PEG / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.06 Å3/Da / Density % sol: 40.4 % / Description: NONE |
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Crystal grow | Temperature: 281 K / Method: vapor diffusion / pH: 5.5 Details: PROTEIN WAS AT 10 MG/ML. THE RESERVOIR CONDITIONS WERE: 40% PEG 600, 100 MM SODIUM CITRATE AT PH 5.5 SET UP AT 8C. CROSS SEEDING FROM OTHER MUTANT CA-II CRYSTALS WAS USED TO OBTAIN THESE CRYSTALS. |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Dec 20, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9537 Å / Relative weight: 1 |
Reflection | Resolution: 1.23→42 Å / Num. obs: 66095 / % possible obs: 98.6 % / Observed criterion σ(I): 0 / Redundancy: 7.3 % / Rmerge(I) obs: 0.04 / Net I/σ(I): 28.7 |
Reflection shell | Resolution: 1.23→1.3 Å / Redundancy: 7.2 % / Rmerge(I) obs: 0.32 / Mean I/σ(I) obs: 6.2 / % possible all: 95.2 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 3ML2 Resolution: 1.23→35.76 Å / Cor.coef. Fo:Fc: 0.982 / Cor.coef. Fo:Fc free: 0.971 / SU B: 1.035 / SU ML: 0.021 / Cross valid method: THROUGHOUT / ESU R: 0.036 / ESU R Free: 0.038 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY THERE IS 'EXTRA' ELECTRON DENSITY NEAR ASP129 WHICH MAKES IT LOOK LIKE THIS MIGHT BE GLUTAMIC ACID INSTEAD OF ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY THERE IS 'EXTRA' ELECTRON DENSITY NEAR ASP129 WHICH MAKES IT LOOK LIKE THIS MIGHT BE GLUTAMIC ACID INSTEAD OF ASPARTIC ACID, BUT THE PLASMID SEQUENCE WAS CHECKED AND THE PROTEIN WAS CHECKED BY MASS SPEC AND BOTH SUGGEST THAT THE RESIDUE SHOULD BE ASP.
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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: 11.268 Å2
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Refinement step | Cycle: LAST / Resolution: 1.23→35.76 Å
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Refine LS restraints |
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