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- PDB-1ezz: CRYSTAL STRUCTURE OF E. COLI ASPARTATE TRANSCARBAMOYLASE P268A MU... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1ezz | ||||||
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Title | CRYSTAL STRUCTURE OF E. COLI ASPARTATE TRANSCARBAMOYLASE P268A MUTANT IN THE T-STATE | ||||||
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![]() | TRANSFERASE / aspartate transcarbamoylase / aspartate carbamoyltransferase / cis-proline / cis-amino acid | ||||||
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 | ![]() | ||||||
![]() | Jin, L. / Stec, B. / Kantrowitz, E.R. | ||||||
![]() | ![]() Title: A cis-proline to alanine mutant of E. coli aspartate transcarbamoylase: kinetic studies and three-dimensional crystal structures. Authors: Jin, L. / 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 | ![]() | 194.4 KB | Display | ![]() |
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PDB format | ![]() | 154.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 421.1 KB | Display | ![]() |
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Full document | ![]() | 479.8 KB | Display | |
Data in XML | ![]() | 27.3 KB | Display | |
Data in CIF | ![]() | 41 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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 | The biological assembly is a dodecamer. The entire molecule requires two symmetry partners generated by rotations around the three-fold |
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Components
#1: Protein | Mass: 34311.070 Da / Num. of mol.: 2 / Mutation: P268A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Plasmid: PEK412, A PLASMID WITH THE PYRBI GENES INSERTED INTO PUC119 Production host: ![]() ![]() #2: Protein | Mass: 17143.625 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Plasmid: PEK412, A PLASMID WITH THE PYRBI GENES INSERTED INTO PUC119 Production host: ![]() ![]() #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.13 Å3/Da / Density % sol: 60.66 % | ||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7 Details: ENZYME: 24 mg/ml; 1:1 enzyme to-buffer ratio, BUFFER: 20 mm HEPES, 14% (w/v) PEG 1450, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K | ||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ | ||||||||||||||||||||
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 III / Detector: AREA DETECTOR / Date: Jun 19, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→30 Å / Num. all: 34450 / Num. obs: 34422 / % possible obs: 99.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.2 % / Biso Wilson estimate: 41.1 Å2 / Rmerge(I) obs: 0.073 / Net I/σ(I): 4.296 |
Reflection shell | Resolution: 2.7→2.91 Å / Redundancy: 2.17 % / Rmerge(I) obs: 0.427 / Num. unique all: 13768 / % possible all: 99.8 |
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Processing
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Refinement | Resolution: 2.7→8 Å / σ(F): 2 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.7→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | |||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.7 Å / Lowest resolution: 8 Å / σ(F): 2 / Rfactor obs: 0.182 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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