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Yorodumi- PDB-1szu: The structure of gamma-aminobutyrate aminotransferase mutant: V241A -
+Open data
-Basic information
Entry | Database: PDB / ID: 1szu | ||||||
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Title | The structure of gamma-aminobutyrate aminotransferase mutant: V241A | ||||||
Components | 4-aminobutyrate aminotransferase | ||||||
Keywords | TRANSFERASE / GABA-AT | ||||||
Function / homology | Function and homology information 5-aminovalerate transaminase / 5-aminovalerate transaminase activity / 4-aminobutyrate-2-oxoglutarate transaminase / 4-aminobutyrate:2-oxoglutarate transaminase activity / N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity / 4-aminobutyrate transaminase activity / gamma-aminobutyric acid catabolic process / arginine biosynthetic process via ornithine / pyridoxal phosphate binding / protein homodimerization activity / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.52 Å | ||||||
Authors | Liu, W. / Peterson, P.E. / Langston, J.A. / Jin, X. / Zhou, X. / Fisher, A.J. / Toney, M.D. | ||||||
Citation | Journal: Biochemistry / Year: 2005 Title: Kinetic and Crystallographic Analysis of Active Site Mutants of Escherichia coligamma-Aminobutyrate Aminotransferase. Authors: Liu, W. / Peterson, P.E. / Langston, J.A. / Jin, X. / Zhou, X. / Fisher, A.J. / Toney, M.D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1szu.cif.gz | 341 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1szu.ent.gz | 289.7 KB | Display | PDB format |
PDBx/mmJSON format | 1szu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1szu_validation.pdf.gz | 523.3 KB | Display | wwPDB validaton report |
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Full document | 1szu_full_validation.pdf.gz | 554.1 KB | Display | |
Data in XML | 1szu_validation.xml.gz | 72.8 KB | Display | |
Data in CIF | 1szu_validation.cif.gz | 101.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/sz/1szu ftp://data.pdbj.org/pub/pdb/validation_reports/sz/1szu | HTTPS FTP |
-Related 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
-Protein , 1 types, 4 molecules ABCD
#1: Protein | Mass: 45799.445 Da / Num. of mol.: 4 / Mutation: V241A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: GABT, B2662 / Production host: Escherichia coli (E. coli) References: UniProt: P22256, 4-aminobutyrate-2-oxoglutarate transaminase |
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-Non-polymers , 5 types, 988 molecules
#2: Chemical | ChemComp-SO4 / #3: Chemical | ChemComp-EDO / #4: Chemical | ChemComp-PLP / #5: Chemical | ChemComp-PMP / #6: 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: 2.78 Å3/Da / Density % sol: 55 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.6 Details: HEPES, ammonium sulfate, PLP, pH 7.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL9-1 / Wavelength: 0.98 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Oct 18, 2000 |
Radiation | Monochromator: Ni filter / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Resolution: 2.52→30 Å / Num. all: 70093 / Num. obs: 68806 / % possible obs: 98.2 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 |
Reflection shell | Highest resolution: 2.52 Å / % possible all: 98.2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.52→30 Å / σ(F): 2 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.52→30 Å
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Refine LS restraints |
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