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- PDB-6hl7: Crystal structure of truncated aspartate transcarbamoylase from P... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6hl7 | |||||||||
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Title | Crystal structure of truncated aspartate transcarbamoylase from Plasmodium falciparum with mutated active site (R109A/K138A) and N-carbamoyl-L-phosphate bound | |||||||||
![]() | Aspartate transcarbamoylase | |||||||||
![]() | TRANSFERASE / Falciparum Malaria Pyrimidine biosynthesis Trimer Mutant TRANSFERASE carbamoyl-phospahte | |||||||||
Function / homology | ![]() aspartate carbamoyltransferase / aspartate carbamoyltransferase activity / amino acid metabolic process / amino acid binding / 'de novo' UMP biosynthetic process / 'de novo' pyrimidine nucleobase biosynthetic process / membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Bosch, S.S. / Lunev, S. / Wrenger, C. / Groves, M.R. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Molecular Target Validation of Aspartate Transcarbamoylase fromPlasmodium falciparumby Torin 2. Authors: Bosch, S.S. / Lunev, S. / Batista, F.A. / Linzke, M. / Kronenberger, T. / Domling, A.S.S. / Groves, M.R. / Wrenger, C. #1: ![]() Title: Crystal structure of truncated aspartate transcarbamoylase from Plasmodium falciparum. Authors: Lunev, S. / Bosch, S.S. / de Assis Batista, F. / Wrenger, C. / Groves, M.R. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 205.7 KB | Display | ![]() |
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PDB format | ![]() | 165 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 470.5 KB | Display | ![]() |
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Full document | ![]() | 494.9 KB | Display | |
Data in XML | ![]() | 36.4 KB | Display | |
Data in CIF | ![]() | 50.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5ilqS 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: 40119.465 Da / Num. of mol.: 3 / Mutation: R109A, K138A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: ATCase / Production host: ![]() ![]() #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.06 Å3/Da / Density % sol: 59.76 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion Details: 0.2M Potassium citrate tribasic monohydrate 20% w/v PEG 3350 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Apr 3, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.976 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→57.61 Å / Num. obs: 46404 / % possible obs: 97.6 % / Observed criterion σ(I): 1.3 / Redundancy: 3.16 % / CC1/2: 0.999 / Rrim(I) all: 0.066 / Net I/σ(I): 12.95 |
Reflection shell | Resolution: 2.5→2.64 Å / Redundancy: 3.21 % / Num. unique obs: 7154 / CC1/2: 0.619 / Rrim(I) all: 0.957 / % possible all: 94 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 5ilq Resolution: 2.5→57.61 Å / Cor.coef. Fo:Fc: 0.956 / Cor.coef. Fo:Fc free: 0.928 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.432 / ESU R Free: 0.283 Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 163.5 Å2 / Biso mean: 65.452 Å2 / Biso min: 28.67 Å2
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Refinement step | Cycle: final / Resolution: 2.5→57.61 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.502→2.567 Å / Total num. of bins used: 20
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