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- PDB-1za2: Structure of wild-type E. coli Aspartate Transcarbamoylase in the... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1za2 | ||||||
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Title | Structure of wild-type E. coli Aspartate Transcarbamoylase in the presence of CTP, carbamoyl phosphate at 2.50 A resolution | ||||||
![]() | (Aspartate carbamoyltransferase ...) x 2 | ||||||
![]() | TRANSFERASE / ordered substrate binding / cooperativity | ||||||
Function / homology | ![]() aspartate carbamoyltransferase complex / pyrimidine nucleotide biosynthetic process / aspartate carbamoyltransferase / aspartate carbamoyltransferase activity / amino acid metabolic process / amino acid binding / glutamine metabolic process / protein homotrimerization / 'de novo' UMP biosynthetic process / 'de novo' pyrimidine nucleobase biosynthetic process ...aspartate carbamoyltransferase complex / pyrimidine nucleotide biosynthetic process / aspartate carbamoyltransferase / aspartate carbamoyltransferase activity / amino acid metabolic process / 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 / metal ion binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Wang, J. / Stieglitz, K.A. / Cardia, J.P. / Kantrowitz, E.R. | ||||||
![]() | ![]() Title: Structural basis for ordered substrate binding and cooperativity in aspartate transcarbamoylase Authors: Wang, J. / Stieglitz, K.A. / Cardia, J.P. / Kantrowitz, E.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 | ![]() | 197.7 KB | Display | ![]() |
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PDB format | ![]() | 156.7 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 | ![]() | 42.3 KB | Display | |
Data in CIF | ![]() | 58.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1za1C ![]() 1tu0S 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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1 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
-Aspartate carbamoyltransferase ... , 2 types, 4 molecules ACBD
#1: Protein | Mass: 34337.105 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P00479, UniProt: P0A786*PLUS, aspartate carbamoyltransferase #2: Protein | Mass: 17143.625 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Non-polymers , 5 types, 390 molecules ![](data/chem/img/NA.gif)
![](data/chem/img/CP.gif)
![](data/chem/img/ZN.gif)
![](data/chem/img/CTP.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/CP.gif)
![](data/chem/img/ZN.gif)
![](data/chem/img/CTP.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | ChemComp-NA / | ||||||
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#4: Chemical | ChemComp-CP / #5: Chemical | #6: Chemical | #7: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.87 Å3/Da / Density % sol: 56.77 % |
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Crystal grow | Temperature: 293 K / Method: microdialysis / pH: 5.7 Details: 40 mM Citric acid, 3 mM sodium azide, 1mM 2-mercaptoethanol, 1mM CTP, 0.2mM EDTA, pH 5.7, MICRODIALYSIS, temperature 293K |
-Data collection
Diffraction source | Source: ![]() ![]() ![]() |
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Detector | Type: ADSC QUANTAM Q315 / Detector: CCD / Date: Aug 22, 2004 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.1 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→30 Å / Num. all: 42642 / Num. obs: 42599 / % possible obs: 99.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 9 % / Rmerge(I) obs: 0.068 / Net I/σ(I): 36.7 |
Reflection shell | Resolution: 2.5→2.59 Å / Redundancy: 8.1 % / Rmerge(I) obs: 0.447 / Mean I/σ(I) obs: 3.8 / % possible all: 99 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB entry 1TU0 Resolution: 2.5→30 Å / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.5→30 Å
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