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Yorodumi- PDB-2d32: Crystal Structure of Michaelis Complex of gamma-Glutamylcysteine ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2d32 | ||||||
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Title | Crystal Structure of Michaelis Complex of gamma-Glutamylcysteine Synthetase | ||||||
Components | Glutamate--cysteine ligase | ||||||
Keywords | LIGASE / glutathione homeostasis / peptide synthesis / phosphoryl transfer | ||||||
Function / homology | Function and homology information glutamate-cysteine ligase / glutamate-cysteine ligase activity / cellular response to mercury ion / glutathione biosynthetic process / cellular response to arsenic-containing substance / hyperosmotic response / ATP binding / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å | ||||||
Authors | Hibi, T. / Nakayama, M. / Nii, H. / Kurokawa, Y. / Katano, H. / Oda, J. | ||||||
Citation | Journal: To be Published Title: Structural basis of efficient coupling peptide ligation and ATP hydrolysis by gamma-gluatamylcysteine synthetase Authors: Hibi, T. / Nakayama, M. / Nii, H. / Kurokawa, Y. / Katano, H. / Oda, J. #1: Journal: Proc.Natl.Acad.Sci.USA / Year: 2004 Title: Crystal structure of gamma-glutamylcysteine synthetase: insights into the mechanism of catalysis by a key enzyme for glutathione homeostasis. Authors: Hibi, T. / Nii, H. / Nakatsu, T. / Kimura, A. / Kato, H. / Hiratake, J. / Oda, J. #2: Journal: Acta Crystallogr.,Sect.D / Year: 2002 Title: Escherichia coli B gamma-glutamylcysteine synthetase: modification, purification, crystallization and preliminary crystallographic analysis. Authors: Hibi, T. / Hisada, H. / Nakatsu, T. / Kato, H. / Oda, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2d32.cif.gz | 422.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2d32.ent.gz | 340.9 KB | Display | PDB format |
PDBx/mmJSON format | 2d32.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/d3/2d32 ftp://data.pdbj.org/pub/pdb/validation_reports/d3/2d32 | HTTPS FTP |
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-Related structure data
Related structure data | 1v4gS 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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2 |
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Unit cell |
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-Components
-Protein , 1 types, 4 molecules ABCD
#1: Protein | Mass: 58268.844 Da / Num. of mol.: 4 / Mutation: C106S, C164S, C205S, C223S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: gshI / Plasmid: pKGC20 / Production host: Escherichia coli (E. coli) / Strain (production host): JM109 / References: UniProt: P0A6W9, glutamate-cysteine ligase |
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-Non-polymers , 5 types, 825 molecules
#2: Chemical | ChemComp-MG / #3: Chemical | ChemComp-GLU / #4: Chemical | ChemComp-CYS / #5: Chemical | ChemComp-ANP / #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: 4.77 Å3/Da / Density % sol: 74 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: sodium formate, Tris-HCl, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL38B1 / Wavelength: 0.9 Å |
Detector | Type: RIGAKU / Detector: IMAGE PLATE / Date: Apr 14, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→43.6 Å / Num. obs: 162223 / % possible obs: 100 % / Redundancy: 8.1 % / Biso Wilson estimate: 50.5 Å2 / Rmerge(I) obs: 0.088 / Net I/σ(I): 6.1 |
Reflection shell | Resolution: 2.4→2.53 Å / Redundancy: 7.9 % / Rmerge(I) obs: 0.374 / Mean I/σ(I) obs: 2 / Num. unique all: 23722 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1V4G Resolution: 2.4→40 Å / Cor.coef. Fo:Fc: 0.958 / Cor.coef. Fo:Fc free: 0.942 / SU B: 9.086 / SU ML: 0.111 / Cross valid method: THROUGHOUT / ESU R: 0.181 / ESU R Free: 0.16 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 45.908 Å2
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Refine analyze | Luzzati coordinate error obs: 0.276 Å / Luzzati d res low obs: 5 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.4→40 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.4→2.462 Å / Total num. of bins used: 20
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