[English] 日本語
Yorodumi- PDB-1r0b: Aspartate Transcarbamylase (ATCase) of Escherichia coli: A New Cr... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1r0b | ||||||
---|---|---|---|---|---|---|---|
Title | Aspartate Transcarbamylase (ATCase) of Escherichia coli: A New Crystalline R State Bound to PALA, or to Product Analogues Phosphate and Citrate | ||||||
Components | (Aspartate carbamoyltransferase ...) x 2 | ||||||
Keywords | TRANSFERASE / Aspartate Transcarbamylase / Aspartate Carbamoyltransferase / product analogue / citrate / phosphate / ATCase-citrate-phosphate Complex / R state | ||||||
Function / homology | Function and homology information 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 / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.9 Å | ||||||
Authors | Huang, J. / Lipscomb, W.N. | ||||||
Citation | Journal: Biochemistry / Year: 2004 Title: Aspartate Transcarbamylase (ATCase) of Escherichia coli: A New Crystalline R-State Bound to PALA, or to Product Analogues Citrate and Phosphate Authors: Huang, J. / Lipscomb, W.N. #1: Journal: Proteins / Year: 1999 Title: Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate ...Title: Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate at 2.1A Authors: Jin, L. / Stec, B. / Lipscomb, W.N. / Kantrowitz, E.R. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1r0b.cif.gz | 558 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1r0b.ent.gz | 455.4 KB | Display | PDB format |
PDBx/mmJSON format | 1r0b.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/r0/1r0b ftp://data.pdbj.org/pub/pdb/validation_reports/r0/1r0b | HTTPS FTP |
---|
-Related structure data
Related structure data | 1q95SC S: Starting model for refinement C: citing same article (ref.) |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-Components
-Aspartate carbamoyltransferase ... , 2 types, 12 molecules ABCDEFGHIJKL
#1: Protein | Mass: 34337.105 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) Gene: PYRB OR B4245 OR C5345 OR Z5856 OR ECS5222 OR SF4245 OR S4507 Plasmid: pEK54 / Production host: Escherichia coli (E. coli) / Strain (production host): EK1104 / References: UniProt: P0A786, aspartate carbamoyltransferase #2: Protein | Mass: 17143.625 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: PYRI OR B4244 OR C5344 OR Z5855 OR ECS5221 / Plasmid: pEK54 / Production host: Escherichia coli (E. coli) / Strain (production host): EK1104 / References: UniProt: P0A7F3 |
---|
-Non-polymers , 4 types, 906 molecules
#3: Chemical | ChemComp-FLC / #4: Chemical | ChemComp-PO4 / #5: Chemical | ChemComp-ZN / #6: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.96 Å3/Da / Density % sol: 58.42 % |
---|---|
Crystal grow | Temperature: 294 K / Method: microdialysis / pH: 5.8 Details: sodium citrate, sodium phosphate, N-ethylmorpholine, pH 5.8, MICRODIALYSIS, temperature 294K |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: CHESS / Beamline: F1 / Wavelength: 0.928 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: May 12, 2002 / Details: mirrors |
Radiation | Monochromator: Horizontally bent si(111), assymetrically cut with water coooled Cu block Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.928 Å / Relative weight: 1 |
Reflection | Resolution: 2.9→50 Å / Num. all: 81814 / Num. obs: 61088 / % possible obs: 74.7 % / Observed criterion σ(I): -0.9 / Redundancy: 3 % / Biso Wilson estimate: 57.6 Å2 / Rsym value: 0.077 / Net I/σ(I): 13.3 |
Reflection shell | Resolution: 2.9→3 Å / Redundancy: 2 % / Mean I/σ(I) obs: 1.8 / Num. unique all: 5461 / Rsym value: 0.46 / % possible all: 75.6 |
-Processing
Software |
| |||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1Q95 Resolution: 2.9→50 Å / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
| |||||||||||||||||||||||||
Displacement parameters | Biso mean: 63.7 Å2
| |||||||||||||||||||||||||
Refine analyze |
| |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.9→50 Å
| |||||||||||||||||||||||||
Refine LS restraints |
| |||||||||||||||||||||||||
LS refinement shell | Resolution: 2.9→3 Å
|