+Open data
-Basic information
Entry | Database: PDB / ID: 9atc | ||||||
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Title | ATCASE Y165F MUTANT | ||||||
Components | (ASPARTATE TRANSCARBAMOYLASE) x 2 | ||||||
Keywords | TRANSFERASE / ATCASE / ALLOSTERY / PYRIMIDINE BIOSYNTHESIS | ||||||
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 / molecular replacement / Resolution: 2.4 Å | ||||||
Authors | Ha, Y. / Allewell, N.M. | ||||||
Citation | Journal: Proteins / Year: 1998 Title: Intersubunit hydrogen bond acts as a global molecular switch in Escherichia coli aspartate transcarbamoylase. Authors: Ha, Y. / Allewell, N.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 9atc.cif.gz | 97.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb9atc.ent.gz | 73.9 KB | Display | PDB format |
PDBx/mmJSON format | 9atc.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/at/9atc ftp://data.pdbj.org/pub/pdb/validation_reports/at/9atc | HTTPS FTP |
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-Related structure data
Related structure data | 1raiS 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
#1: Protein | Mass: 34321.109 Da / Num. of mol.: 1 / Mutation: CHAIN A, Y165F Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Plasmid: PEK33 / Production host: Escherichia coli (E. coli) / Strain (production host): EK1104 / References: UniProt: P0A786, aspartate carbamoyltransferase |
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#2: Protein | Mass: 16301.649 Da / Num. of mol.: 1 / Mutation: CHAIN A, Y165F Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Plasmid: PEK33 / Production host: Escherichia coli (E. coli) / Strain (production host): EK1104 / References: UniProt: P0A7F3, aspartate carbamoyltransferase |
#3: Chemical | ChemComp-ZN / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 4 |
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-Sample preparation
Crystal | Density Matthews: 3.25 Å3/Da / Density % sol: 62.13 % | |||||||||||||||||||||||||
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Crystal grow | pH: 6.3 / Details: pH 6.3 | |||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 18 ℃ / pH: 7.45 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 300 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RUH2R / Wavelength: 1.5418 |
Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: Jun 1, 1994 |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→10 Å / Num. obs: 21881 / % possible obs: 83 % / Observed criterion σ(I): 2 / Rsym value: 0.074 / Net I/σ(I): 14.3 |
Reflection shell | Resolution: 2.34→2.48 Å / Mean I/σ(I) obs: 1.6 / Rsym value: 0.133 / % possible all: 42 |
Reflection | *PLUS Num. measured all: 160964 / Rmerge(I) obs: 0.074 |
Reflection shell | *PLUS % possible obs: 42 % / Num. unique obs: 1980 / Num. measured obs: 3260 / Rmerge(I) obs: 0.133 |
-Processing
Software |
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Refinement | Method to determine structure: molecular replacement Starting model: ATCASE WILDTYPE T (1RAI) Resolution: 2.4→10 Å / Data cutoff high absF: 10000 / Data cutoff low absF: 0.1 / Cross valid method: THROUGHOUT / σ(F): 2
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Refinement step | Cycle: LAST / Resolution: 2.4→10 Å
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Refine LS restraints |
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Xplor file |
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Software | *PLUS Name: X-PLOR / Version: 3.8 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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