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- PDB-1i5o: CRYSTAL STRUCTURE OF MUTANT R105A OF E. COLI ASPARTATE TRANSCARBA... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1i5o | ||||||
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Title | CRYSTAL STRUCTURE OF MUTANT R105A OF E. COLI ASPARTATE TRANSCARBAMOYLASE | ||||||
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![]() | TRANSFERASE / Mutant aspartate transcarbamoylase / T-state / PALA at the regulatory site | ||||||
Function / homology | ![]() aspartate carbamoyltransferase complex / pyrimidine nucleotide biosynthetic process / aspartate carbamoyltransferase / aspartate carbamoyltransferase activity / amino acid binding / glutamine metabolic process / protein homotrimerization / 'de novo' UMP biosynthetic process / 'de novo' pyrimidine nucleobase biosynthetic process / zinc ion binding ...aspartate carbamoyltransferase complex / pyrimidine nucleotide biosynthetic process / aspartate carbamoyltransferase / aspartate carbamoyltransferase activity / amino acid binding / glutamine metabolic process / protein homotrimerization / 'de novo' UMP biosynthetic process / 'de novo' pyrimidine nucleobase biosynthetic process / zinc ion binding / identical protein binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Macol, C.P. / Tsuruta, H. / Stec, B. / Kantrowitz, E.R. | ||||||
![]() | ![]() Title: Direct structural evidence for a concerted allosteric transition in Escherichia coli aspartate transcarbamoylase. Authors: Macol, C.P. / Tsuruta, H. / Stec, B. / Kantrowitz, E.R. #1: ![]() Title: Structural Consequences of Effector Binding to the T State of Aspartate Carbamoyltransferase: Crystal Structures of the Unligated and ATP- and CTP-complexed Enzymes at 2.6-A Resolution. Authors: Stevens, R.C. / Gouaux, J.E. / Lipscomb, W.N. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 195.2 KB | Display | ![]() |
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PDB format | ![]() | 154.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 675.9 KB | Display | ![]() |
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Full document | ![]() | 712.9 KB | Display | |
Data in XML | ![]() | 41.7 KB | Display | |
Data in CIF | ![]() | 58.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5at1S 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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1 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Details | Deposited data for two catalytic and two regulatory chains Biological assembly: dodecamer can be obtained by application of the threefold crystallographic symmetry |
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Components
#1: Protein | Mass: 34250.992 Da / Num. of mol.: 2 / Mutation: R105A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Protein | Mass: 17143.625 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #3: Chemical | #4: Chemical | ChemComp-PAL / | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.99 Å3/Da / Density % sol: 58.9 % | |||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: microdialysis / pH: 5.7 Details: Tris buffer, maleic acid, pH 5.7, MICRODIALYSIS, temperature 293K | |||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / pH: 5.75 / Details: Jin, L., (2000) Biochemistry, 39, 8058. | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 295 K |
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Diffraction source | Source: ![]() |
Detector | Type: UCSD MARK II / Detector: AREA DETECTOR / Date: Jul 25, 1996 |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.78→30 Å / Num. all: 29390 / Num. obs: 29390 / % possible obs: 93 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.08 % / Biso Wilson estimate: 26.54 Å2 / Rmerge(I) obs: 0.099 / Net I/σ(I): 5.75 |
Reflection shell | Resolution: 2.78→2.99 Å / Redundancy: 1.85 % / Rmerge(I) obs: 0.37 / Mean I/σ(I) obs: 1 / Num. unique all: 4622 / % possible all: 75 |
Reflection | *PLUS Num. measured all: 90537 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 5at1 Resolution: 2.8→10 Å / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / σ(F): 2 / σ(I): 1 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 31.2 Å2 | |||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.25 Å | |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.8→10 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.8→2.9 Å
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Software | *PLUS Name: ![]() | |||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 10 Å / σ(F): 2 / % reflection Rfree: 10 % / Rfactor all: 0.157 / Rfactor obs: 0.155 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 31.2 Å2 | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 2.9 Å |