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- PDB-2gtu: LIGAND-FREE HUMAN GLUTATHIONE S-TRANSFERASE M2-2 (E.C.2.5.1.18), ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2gtu | ||||||
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Title | LIGAND-FREE HUMAN GLUTATHIONE S-TRANSFERASE M2-2 (E.C.2.5.1.18), MONOCLINIC CRYSTAL FORM | ||||||
![]() | GLUTATHIONE S-TRANSFERASE | ||||||
![]() | TRANSFERASE / GLUTATHIONE / CONJUGATION / DETOXIFICATION / CYTOSOLIC / DIMER | ||||||
Function / homology | ![]() nitrobenzene metabolic process / cellular detoxification of nitrogen compound / regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion / glutathione binding / hepoxilin biosynthetic process / linoleic acid metabolic process / Glutathione conjugation / glutathione peroxidase activity / relaxation of cardiac muscle / intercellular bridge ...nitrobenzene metabolic process / cellular detoxification of nitrogen compound / regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion / glutathione binding / hepoxilin biosynthetic process / linoleic acid metabolic process / Glutathione conjugation / glutathione peroxidase activity / relaxation of cardiac muscle / intercellular bridge / positive regulation of ryanodine-sensitive calcium-release channel activity / cellular response to caffeine / glutathione transferase / glutathione transferase activity / negative regulation of ryanodine-sensitive calcium-release channel activity / regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion / xenobiotic catabolic process / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / glutathione metabolic process / sarcoplasmic reticulum / fatty acid binding / signaling receptor binding / enzyme binding / protein homodimerization activity / extracellular exosome / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Patskovska, L.N. / Fedorov, A.A. / Patskovsky, Y.V. / Almo, S.C. / Listowsky, I. | ||||||
![]() | ![]() Title: The enhanced affinity for thiolate anion and activation of enzyme-bound glutathione is governed by an arginine residue of human Mu class glutathione S-transferases. Authors: Patskovsky, Y.V. / Patskovska, L.N. / Listowsky, I. #1: ![]() Title: Expression, Crystallization and Preliminary X-Ray Analysis of Ligand-Free Human Glutathione S-Transferase M2-2 Authors: Patskovska, L.N. / Fedorov, A.A. / Patskovsky, Y.V. / Almo, S.C. / Listowsky, I. #2: ![]() Title: Crystal Structure of Human Class Mu Glutathione Transferase Gstm2-2. Effects of Lattice Packing on Conformational Heterogeneity Authors: Raghunathan, S. / Chandross, R.J. / Kretsinger, R.H. / Allison, T.J. / Penington, C.J. / Rule, G.S. #3: ![]() Title: Cloning, Expression, and Characterization of a Class-Mu Glutathione Transferase from Human Muscle, the Product of the Gst4 Locus Authors: Vorachek, W.R. / Pearson, W.R. / Rule, G.S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 99.1 KB | Display | ![]() |
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PDB format | ![]() | 77.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 420.7 KB | Display | ![]() |
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Full document | ![]() | 428.2 KB | Display | |
Data in XML | ![]() | 17.7 KB | Display | |
Data in CIF | ![]() | 23.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1hnaS S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.187925, 0.958163, 0.215887), Vector: |
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Components
#1: Protein | Mass: 25645.457 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: LIGAND-FREE / Source: (gene. exp.) ![]() Description: THE GSTM2 CDNA WAS AMPLIFIED USING RT-PCR AND SUBCLONED INTO A PET3A EXPRESSION VECTOR Cell line: HELA / Cellular location: CYTOPLASM / Gene: GSTM2 / Plasmid: PET3A-GSTM2 / Species (production host): Escherichia coli / Gene (production host): GSTM2 / Production host: ![]() ![]() #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.23 Å3/Da / Density % sol: 45 % | ||||||||||||||||||||||||
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Crystal grow | pH: 8.5 / Details: pH 8.5 | ||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.5 / Method: vapor diffusion, hanging dropDetails: Patskovska, L.N., (1998) Acta Crystallogr.,Sect.D, 54, 458. | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 289 K |
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Diffraction source | Source: ![]() |
Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: Mar 1, 1997 |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.55→10 Å / Num. obs: 12321 / % possible obs: 84.15 % / Observed criterion σ(I): 2 / Redundancy: 1.9 % / Rmerge(I) obs: 0.051 / Net I/σ(I): 13.5 |
Reflection shell | Resolution: 2.55→3 Å / Redundancy: 1.55 % / Rmerge(I) obs: 0.097 / Mean I/σ(I) obs: 4.2 / % possible all: 48 |
Reflection | *PLUS Rmerge(I) obs: 0.051 |
Reflection shell | *PLUS Rmerge(I) obs: 0.097 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1HNA Resolution: 2.55→10 Å / Rfactor Rfree error: 0.007 / Data cutoff high absF: 1000000 / Data cutoff low absF: 0.001 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.55→10 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.55→2.66 Å / Rfactor Rfree error: 0.01 / Total num. of bins used: 8
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Xplor file |
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Refinement | *PLUS Rfactor obs: 0.203 / Rfactor Rfree: 0.257 / Rfactor Rwork: 0.203 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.315 / Rfactor Rwork: 0.243 / Rfactor obs: 0.243 |