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Open data
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Basic information
Entry | Database: PDB / ID: 2glt | |||||||||
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Title | STRUCTURE OF ESCHERICHIA COLI GLUTATHIONE SYNTHETASE AT PH 6.0. | |||||||||
![]() | GLUTATHIONE BIOSYNTHETIC LIGASE | |||||||||
![]() | BIOSYNTHESIS / LIGASE / GLUTATHIONE BIOSYNTHESIS LIGASE | |||||||||
Function / homology | ![]() glutathione synthase / glutathione synthase activity / glutathione biosynthetic process / protein homotetramerization / magnesium ion binding / ATP binding / identical protein binding / cytoplasm / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Matsuda, K. / Yamaguchi, H. / Kato, H. / Nishioka, T. / Katsube, Y. / Oda, J. | |||||||||
![]() | ![]() Title: Crystal structure of glutathione synthetase at optimal pH: domain architecture and structural similarity with other proteins. Authors: Matsuda, K. / Mizuguchi, K. / Nishioka, T. / Kato, H. / Go, N. / Oda, J. #1: ![]() Title: Flexible Loop that is Novel Catalytic Machinery in a Ligase. Atomic Structure and Function of the Loopless Glutathione Synthetase Authors: Kato, H. / Tanaka, T. / Yamaguchi, H. / Hara, T. / Nishioka, T. / Katsube, Y. / Oda, J. #2: ![]() Title: Mechanism-Based Inactivation of Glutathione Synthetase by Phosphinic Acid Transition-State Analogue Authors: Hiratake, J. / Kato, H. / Oda, J. #3: ![]() Title: Use of Adenosine (5')Polyphospho(5')Pyridoxals to Study the Substrate-Binding Region of Glutathione Synthetase from Escherichia Coli B Authors: Hibi, T. / Kato, H. / Nishioka, T. / Oda, J. / Yamaguchi, H. / Katsube, Y. / Tanizawa, K. / Fukui, T. #4: ![]() Title: Flexibility Impaired by Mutations Revealed the Multi-Functional Roles of the Loop in Glutathione Synthetase Authors: Tanaka, T. / Yamaguchi, H. / Kato, H. / Nishioka, T. / Katsube, Y. / Oda, J. #5: ![]() Title: Three-Dimensional Structure of the Glutathione Synthetase from Escherichia Coli B at 2.0 Angstroms Resolution Authors: Yamaguchi, H. / Kato, H. / Hata, Y. / Nishioka, T. / Kimura, A. / Oda, J. / Katsube, Y. #6: ![]() Title: Construction, Expression, and Characterization of Glutathione Synthetase Chimeras: Substitution of a Homologous Loop Peptide Region of Dihydrofolate Reductase Authors: Tanaka, T. / Sakai, T. / Chihara-Siomi, M. / Takeshima, K. / Kato, H. / Misawa, T. / Nishioka, T. / Oda, J. #7: ![]() Title: Mutational and Proteolytic Studies on a Flexible Loop in Glutathione Synthetase from Escherichia Coli B: The Loop and Arginine 233 are Critical for the Catalytic Reaction Authors: Tanaka, T. / Kato, H. / Nishioka, T. / Oda, J. #8: ![]() Title: Structural Studies on Glutathione Synthetase from Escherichia Coli B Authors: Yamaguchi, H. / Kato, H. / Hata, Y. / Nishioka, T. / Oda, J. / Katsube, Y. #9: ![]() Title: Crystallization and Preliminary X-Ray Studies of Glutathione Synthetase from Escherichia Coli B Authors: Kato, H. / Yamaguchi, H. / Hata, Y. / Nishioka, T. / Katsube, Y. / Oda, J. #10: ![]() Title: Overexpression of Glutathione Synthase in Escherichia Coli Authors: Kato, H. / Kobayashi, M. / Murata, K. / Nishioka, T. / Oda, J. #11: ![]() Title: Role of Cysteine Residues in Glutathione Synthetase from Escherchia Coli B Authors: Kato, H. / Tanaka, T. / Nishioka, T. / Kimura, A. / Oda, J. #12: ![]() Title: Complete Nucleotide Sequence of E.Coli Glutathione Synthetase Gsh-II Authors: Gushima, H. / Yasuda, S. / Soeda, E. / Yokota, M. / Kondo, M. / Kimura, A. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 73.9 KB | Display | ![]() |
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PDB format | ![]() | 55.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 366.9 KB | Display | ![]() |
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Full document | ![]() | 372 KB | Display | |
Data in XML | ![]() | 7.7 KB | Display | |
Data in CIF | ![]() | 11.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Atom site foot note | 1: CIS PROLINE - PRO 90 2: VAL 113 - ASN 114 OMEGA = 357.86 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION | ||||||||
Details | SYMMETRY THE CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS PRESENTED BELOW GENERATE THE SUBUNITS OF THE POLYMERIC MOLECULE. APPLIED TO RESIDUES: 1 .. 316 SYMMETRY1 1 0.000000 1.000000 0.000000 0.00000 SYMMETRY2 1 1.000000 0.000000 0.000000 0.00000 SYMMETRY3 1 0.000000 0.000000 -1.000000 0.66667 SYMMETRY1 2 -1.000000 0.000000 0.000000 1.00000 SYMMETRY2 2 0.000000 -1.000000 0.000000 1.00000 SYMMETRY3 2 0.000000 0.000000 1.000000 0.00000 SYMMETRY1 3 0.000000 -1.000000 0.000000 1.00000 SYMMETRY2 3 -1.000000 0.000000 0.000000 1.00000 SYMMETRY3 3 0.000000 0.000000 -1.000000 0.66667 |
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Components
#1: Protein | Mass: 35601.824 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.58 Å3/Da / Density % sol: 52.26 % Description: INTENSITY DATA WERE COLLECTED WITH A WEISSENBERG CAMERA EQUIPPED WITH A CYLINDRICAL CASSETTE HAVING A 430 MM RADIUS AND THE FUJI FILM IMAGING PLATES | ||||||||||||||||||||||||
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Crystal grow | *PLUS Method: unknown | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: ![]() ![]() ![]() |
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Detector | Type: WEISSENBERG / Detector: DIFFRACTOMETER / Date: Aug 3, 1990 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.04 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→77.8 Å / Num. obs: 24571 / % possible obs: 84.1 % / Observed criterion σ(I): 1 |
Reflection | *PLUS % possible obs: 77.8 % / Rmerge(I) obs: 0.053 |
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Processing
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Refinement | Resolution: 2.2→10 Å / σ(F): 2
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Displacement parameters | Biso mean: 21.49 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.2→10 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rfree: 0.26 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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