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Yorodumi- PDB-1qis: ASPARTATE AMINOTRANSFERASE FROM ESCHERICHIA COLI, C191F MUTATION,... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1qis | ||||||
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Title | ASPARTATE AMINOTRANSFERASE FROM ESCHERICHIA COLI, C191F MUTATION, WITH BOUND MALEATE | ||||||
Components | ASPARTATE AMINOTRANSFERASE | ||||||
Keywords | AMINOTRANSFERASE / TRANSFERASE(AMINOTRANSFERASE) / PYRIDOXAL PHOSPHATE / MALEATE | ||||||
Function / homology | Function and homology information L-phenylalanine biosynthetic process from chorismate via phenylpyruvate / L-tyrosine-2-oxoglutarate transaminase activity / L-phenylalanine biosynthetic process / aspartate transaminase / L-aspartate:2-oxoglutarate aminotransferase activity / pyridoxal phosphate binding / protein homodimerization activity / identical protein binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ESCHERICHIA COLI (E. coli) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.9 Å | ||||||
Authors | Jeffery, C.J. / Gloss, L.M. / Petsko, G.A. / Ringe, D. | ||||||
Citation | Journal: Protein Eng. / Year: 2000 Title: The Role of Residues Outside the Active Site in Catalysis: Structural Basis for Function of C191 Mutants of E. Coli Aspartate Aminotransferase Authors: Jeffery, C.J. / Gloss, L.M. / Petsko, G.A. / Ringe, D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1qis.cif.gz | 93.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1qis.ent.gz | 69.3 KB | Display | PDB format |
PDBx/mmJSON format | 1qis.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qi/1qis ftp://data.pdbj.org/pub/pdb/validation_reports/qi/1qis | HTTPS FTP |
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-Related structure data
Related structure data | 1b4xC 1qirC 1qitC 5eaaC 1asaS 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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Details | BIOLOGICAL_UNIT: ACTIVE AS A DIMER |
-Components
#1: Protein | Mass: 43663.246 Da / Num. of mol.: 1 / Fragment: COMPLETE SUBUNIT / Mutation: YES Source method: isolated from a genetically manipulated source Details: PYRIDOXAL PHOSPHATE COFACTOR COVALENTLY BOUND TO LYS258 VIA SCHIFF BASE LINKAGE Source: (gene. exp.) ESCHERICHIA COLI (E. coli) / Cellular location: CYTOPLASM / Cellular location (production host): CYTOPLASM / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P00509, aspartate transaminase |
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#2: Chemical | ChemComp-PLP / |
#3: Chemical | ChemComp-MAE / |
#4: Water | ChemComp-HOH / |
Compound details | NUMBERED TO MATCH NUMBERING OF CHICKEN CYTOPLASMI |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3 Å3/Da / Density % sol: 61 % | ||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.5 Details: PROTEIN SOLUTION: 13MG/ML PROTEIN, 20 MM POTASSIUM PHOSPHATE BUFFER, PH 7.5, 10 UM PLP, 5 MM EDTA, RESERVOIR SOLUTION: 20MM POTASSIUM PHOSPHATE BUFFER, PH 7.5, AND 45-50% AMMONIUM SULFATE | ||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 297 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RUH2R / Wavelength: 1.5418 |
Detector | Type: RIGAKU IMAGE PLATE / Detector: IMAGE PLATE |
Radiation | Monochromator: NI FILTER / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→50 Å / Num. obs: 40823 / % possible obs: 90 % / Observed criterion σ(I): 0 / Redundancy: 1 % / Rmerge(I) obs: 0.038 |
Reflection shell | Highest resolution: 1.9 Å |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1ASA Resolution: 1.9→10 Å / Data cutoff high absF: 1000000 / Data cutoff low absF: 0 / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso mean: 26.08 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→10 Å
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Refine LS restraints |
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Xplor file | Serial no: 1 / Param file: PARHCSDX.PRO / Topol file: TOPHCSDX.PRO | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: X-PLOR / Version: 3.851 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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