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Yorodumi- PDB-2qgf: Structure of regulatory chain mutant H20A of asparate transcarbam... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2qgf | ||||||
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Title | Structure of regulatory chain mutant H20A of asparate transcarbamoylase from E. coli | ||||||
Components |
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Keywords | TRANSFERASE/Transferase regulator / allosteric enzyme regulatory chain mutation / heterotropic regulation / TRANSFERASE-Transferase regulator COMPLEX | ||||||
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 / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.2 Å | ||||||
Authors | Stec, B. / Williams, M.K. / Stieglitz, K.A. / Kantrowitz, E.R. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 2007 Title: Comparison of two T-state structures of regulatory-chain mutants of Escherichia coli aspartate transcarbamoylase suggests that His20 and Asp19 modulate the response to heterotropic effectors. Authors: Stec, B. / Williams, M.K. / Stieglitz, K.A. / Kantrowitz, E.R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2qgf.cif.gz | 197.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2qgf.ent.gz | 158.2 KB | Display | PDB format |
PDBx/mmJSON format | 2qgf.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2qgf_validation.pdf.gz | 445 KB | Display | wwPDB validaton report |
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Full document | 2qgf_full_validation.pdf.gz | 465.4 KB | Display | |
Data in XML | 2qgf_validation.xml.gz | 40.5 KB | Display | |
Data in CIF | 2qgf_validation.cif.gz | 57.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qg/2qgf ftp://data.pdbj.org/pub/pdb/validation_reports/qg/2qgf | HTTPS FTP |
-Related structure data
Related structure data | 2qg9C 1nbeS C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-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
#1: Protein | Mass: 34337.105 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: EK1104 / Gene: pyrB / Plasmid: pEK121 / Production host: Escherichia coli (E. coli) / References: UniProt: P0A786, aspartate carbamoyltransferase #2: Protein | Mass: 17076.557 Da / Num. of mol.: 2 / Mutation: H20A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: pyrI / Plasmid: pEK121 / Production host: Escherichia coli (E. coli) / References: UniProt: P0A7F3 #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.99 Å3/Da / Density % sol: 58.86 % |
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Crystal grow | Temperature: 298 K / Method: microdialysis / pH: 5.7 Details: 0.1M citric acid, pH 5.7, MICRODIALYSIS, temperature 298.0K |
-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 Å |
Detector | Type: UCSD MARK II / Detector: AREA DETECTOR / Date: Nov 18, 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: 2.2→35 Å / Num. all: 59318 / Num. obs: 59318 / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.3 % / Rmerge(I) obs: 0.099 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1NBE Resolution: 2.2→35 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: 2.2→35 Å
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Refine LS restraints |
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