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- PDB-1ovd: THE K136E MUTANT OF LACTOCOCCUS LACTIS DIHYDROOROTATE DEHYDROGENA... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ovd | ||||||
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Title | THE K136E MUTANT OF LACTOCOCCUS LACTIS DIHYDROOROTATE DEHYDROGENASE A IN COMPLEX WITH OROTATE | ||||||
![]() | DIHYDROOROTATE DEHYDROGENASE A | ||||||
![]() | OXIDOREDUCTASE / HOMODIMER / ALPHA-BETA BARREL / FLAVOPROTEIN / OROTATE COMPLEX / MUTANT ENZYME | ||||||
Function / homology | ![]() dihydroorotate dehydrogenase (fumarate) / dihydroorotate dehydrogenase (fumarate) activity / 'de novo' UMP biosynthetic process / 'de novo' pyrimidine nucleobase biosynthetic process / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Norager, S. / Arent, S. / Bjornberg, O. / Ottosen, M. / Lo Leggio, L. / Jensen, K.F. / Larsen, S. | ||||||
![]() | ![]() Title: Lactococcus lactis dihydroorotate dehydrogenase A mutants reveal important facets of the enzymatic function. Authors: Norager, S. / Arent, S. / Bjornberg, O. / Ottesen, M. / Lo Leggio, L. / Jensen, K.F. / Larsen, S. #1: ![]() Title: Active Site of Dihydroorotate Dehydrogenase A from Lactococcus Lactis Investigated by Chemical Modification and Mutagenesis Authors: Bjornberg, O. / Rowland, P. / Larsen, S. / Jensen, K.F. #2: ![]() Title: The Crystals Structure of Lactococcus Lactis Dihydroorotate Dehydrogenase A Complexed with the Enzyme Reaction Product Throws Light on its Enzymatic Function Authors: Rowland, P. / Bjornberg, O. / Nielsen, F.S. / Jensen, K.F. / Larsen, S. #3: ![]() Title: The Crystals Structure of the Flavin Containing Enzyme Dihydroorotate Dehydrogenase A from Lactococcus Lactis Authors: Rowland, P. / Nielsen, F.S. / Jensen, K.F. / Larsen, S. #4: ![]() Title: Purification and Characterisation of Dihydroorotate Dehydrogenase A from Lactococcus Lactis, Crystallisation and Preliminary X-Ray Diffraction Studies of the Enzyme Authors: Nielsen, F.S. / Rowland, P. / Larsen, S. / Jensen, K.F. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 146.7 KB | Display | ![]() |
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PDB format | ![]() | 112.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 30.9 KB | Display | |
Data in CIF | ![]() | 44.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1jqvC ![]() 1jqxC ![]() 1jrbC ![]() 1jrcC ![]() 1jubC ![]() 1jueC ![]() 1dorS S: Starting model for refinement C: citing same article ( |
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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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Details | The asymmetric unit contains the biological homodimer |
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Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 34242.102 Da / Num. of mol.: 2 / Mutation: K136E Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: PYRDA / Plasmid: PUHE23 / Production host: ![]() ![]() References: UniProt: P54321, UniProt: A2RJT9*PLUS, EC: 1.3.3.1 |
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-Non-polymers , 5 types, 498 molecules ![](data/chem/img/MG.gif)
![](data/chem/img/FMN.gif)
![](data/chem/img/ORO.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/FMN.gif)
![](data/chem/img/ORO.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | #3: Chemical | #4: Chemical | #5: Chemical | ChemComp-GOL / #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.41 Å3/Da / Density % sol: 48.61 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: PEG 6K, Sodium acetate, Tris-HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7 / Method: vapor diffusion | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Sep 26, 2001 / Details: Bent mirror |
Radiation | Monochromator: Si(III) single crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.098 Å / Relative weight: 1 |
Reflection | Resolution: 2.25→12 Å / Num. all: 34158 / Num. obs: 33990 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 4.3 % / Biso Wilson estimate: 6.2 Å2 / Rmerge(I) obs: 0.089 / Net I/σ(I): 15.3 |
Reflection shell | Resolution: 2.25→2.29 Å / Rmerge(I) obs: 0.282 / Mean I/σ(I) obs: 4.93 / Num. unique all: 1709 / % possible all: 100 |
Reflection | *PLUS Num. obs: 34158 / % possible obs: 100 % / Num. measured all: 146256 |
Reflection shell | *PLUS % possible obs: 100 % / Mean I/σ(I) obs: 4.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: Lactococcus lactis DHODA PDB ID 1DOR Resolution: 2.25→12 Å / Rfactor Rfree error: 0.005 / Data cutoff high absF: 156760.05 / Data cutoff high rms absF: 156760.05 / Data cutoff low absF: 0 / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: ENGH & HUBER
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Solvent computation | Solvent model: FLAT / Bsol: 42.7672 Å2 / ksol: 0.353933 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 19.5 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.25→12 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.25→2.39 Å / Rfactor Rfree error: 0.015 / Total num. of bins used: 10
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Xplor file |
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Refine LS restraints | *PLUS
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