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- PDB-6b4r: The crystal structure of the aldehyde dehydrogenase KauB from Pse... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6b4r | ||||||
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Title | The crystal structure of the aldehyde dehydrogenase KauB from Pseudomonas aeruginosa | ||||||
![]() | (KauB) x 2 | ||||||
![]() | OXIDOREDUCTASE / aldehyde dehydrogenase / KauB | ||||||
Function / homology | ![]() oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Gonzalez-Segura, L. / Cardona-Cardona, Y. / Carrillo-Campos, J. / Munoz-Clares, R.A. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Aldehyde specificity of the aldehyde dehydrogenase KauB from Pseudomonas aeruginosa: Critical amino acid residues revealed by its crystal structure Authors: Cardona-Cardona, Y. / Gonzalez-Segura, L. / Carrillo-Campos, J. / Regla, I. / Lopez-Ortiz, M. / Gutierrez, A. / Munoz-Clares, R.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 | ![]() | 387.4 KB | Display | ![]() |
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PDB format | ![]() | 313.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 486.8 KB | Display | ![]() |
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Full document | ![]() | 497.7 KB | Display | |
Data in XML | ![]() | 70.6 KB | Display | |
Data in CIF | ![]() | 96.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4lihS 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
-Protein , 2 types, 4 molecules ACBD
#1: Protein | Mass: 53233.473 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1 Gene: PA5312 / Plasmid: pET28b-KauB / Production host: ![]() ![]() References: UniProt: Q9HTP2, gamma-guanidinobutyraldehyde dehydrogenase #2: Protein | Mass: 53201.473 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1 Gene: PA5312 / Plasmid: pET28b-KauB / Production host: ![]() ![]() References: UniProt: Q9HTP2, gamma-guanidinobutyraldehyde dehydrogenase |
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-Non-polymers , 5 types, 528 molecules ![](data/chem/img/EDO.gif)
![](data/chem/img/K.gif)
![](data/chem/img/TOE.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/K.gif)
![](data/chem/img/TOE.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | ChemComp-EDO / #4: Chemical | ChemComp-K / #5: Chemical | #6: Chemical | ChemComp-GOL / | #7: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.52 Å3/Da / Density % sol: 51.22 % |
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Crystal grow | Temperature: 291.15 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: 0.17 M SODIUM ACETATE TRIHYDRATE, 0.1 M TRIS HYDROCHLORIDE PH 8.5, 25.5% W/V POLYETHYLENE GLYCOL 4,000, 15% V/V GLYCEROL. |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Oct 20, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97918 Å / Relative weight: 1 |
Reflection | Resolution: 2.55→46.125 Å / Num. obs: 68734 / % possible obs: 99.41 % / Redundancy: 6.3 % / Rmerge(I) obs: 0.111 / Rpim(I) all: 0.049 / Net I/σ(I): 10.5 |
Reflection shell | Resolution: 2.55→2.641 Å / Redundancy: 6.4 % / Rmerge(I) obs: 0.37 / Mean I/σ(I) obs: 4.4 / Num. unique obs: 10041 / Rpim(I) all: 0.158 / % possible all: 99.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 4LIH Resolution: 2.55→46.125 Å / SU ML: 0.31 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 23.57 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.55→46.125 Å
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Refine LS restraints |
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LS refinement shell |
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