+Open data
-Basic information
Entry | Database: PDB / ID: 1g4v | ||||||
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Title | ASPARTATE AMINOTRANSFERASE ACTIVE SITE MUTANT N194A/Y225F | ||||||
Components | ASPARTATE AMINOTRANSFERASEAspartate transaminase | ||||||
Keywords | TRANSFERASE / ACTIVE SITE MUTANT | ||||||
Function / homology | Function and homology information L-phenylalanine biosynthetic process from chorismate via phenylpyruvate / L-tyrosine:2-oxoglutarate aminotransferase 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 / SYNCHROTRON / Resolution: 2 Å | ||||||
Authors | Mizuguchi, H. / Hayashi, H. / Okada, K. / Miyahara, I. / Hirotsu, K. / Kagamiyama, H. | ||||||
Citation | Journal: Biochemistry / Year: 2001 Title: Strain is more important than electrostatic interaction in controlling the pKa of the catalytic group in aspartate aminotransferase. Authors: Mizuguchi, H. / Hayashi, H. / Okada, K. / Miyahara, I. / Hirotsu, K. / Kagamiyama, H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1g4v.cif.gz | 89.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1g4v.ent.gz | 70.7 KB | Display | PDB format |
PDBx/mmJSON format | 1g4v.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/g4/1g4v ftp://data.pdbj.org/pub/pdb/validation_reports/g4/1g4v | HTTPS FTP |
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-Related 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: 43560.188 Da / Num. of mol.: 1 / Mutation: N194A, Y225F Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Production host: Escherichia coli (E. coli) / References: UniProt: P00509, aspartate transaminase |
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#2: Chemical | ChemComp-PLP / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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-Sample preparation
Crystal | Density Matthews: 3.08 Å3/Da / Density % sol: 60.08 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7 Details: Sodium Sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 20.0K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 293 K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: SYNCHROTRON / Site: Photon Factory / Beamline: BL-6A / Wavelength: 1 |
Detector | Type: FUJI / Detector: IMAGE PLATE / Date: Dec 8, 1992 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2→20 Å / Num. all: 92716 / Num. obs: 27638 / Observed criterion σ(F): 3 / Rmerge(I) obs: 0.067 |
Reflection | *PLUS Highest resolution: 2 Å / % possible obs: 91 % / Num. measured all: 92716 |
-Processing
Software |
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Refinement | Resolution: 2→10 Å / σ(F): 3 / Stereochemistry target values: Engh & Huber /
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Refinement step | Cycle: LAST / Resolution: 2→10 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | ||||||||||||||||||
Refinement | *PLUS Highest resolution: 2 Å / Lowest resolution: 10 Å / σ(F): 3 | ||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||
Displacement parameters | *PLUS |