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Yorodumi- PDB-1hna: CRYSTAL STRUCTURE OF HUMAN CLASS MU GLUTATHIONE TRANSFERASE GSTM2... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1hna | ||||||
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Title | CRYSTAL STRUCTURE OF HUMAN CLASS MU GLUTATHIONE TRANSFERASE GSTM2-2: EFFECTS OF LATTICE PACKING ON CONFORMATIONAL HETEROGENEITY | ||||||
Components | GLUTATHIONE S-TRANSFERASE | ||||||
Keywords | TRANSFERASE(GLUTATHIONE) | ||||||
Function / homology | Function and homology information 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 / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.85 Å | ||||||
Authors | Raghunathan, S. / Chandross, R.J. / Kretsinger, R.H. / Allison, T.J. / Penington, C.J. / Rule, G.S. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1994 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. #1: Journal: Biochemistry / Year: 1992 Title: Mapping of the Substrate-Binding Site of a Human Class Mu Glutathione Transferase Using Nuclear Magnetic Resonance Spectroscopy Authors: Penington, C.R. / Rule, G.S. #2: Journal: Proc.Natl.Acad.Sci.USA / Year: 1991 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1hna.cif.gz | 59.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1hna.ent.gz | 43.3 KB | Display | PDB format |
PDBx/mmJSON format | 1hna.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hn/1hna ftp://data.pdbj.org/pub/pdb/validation_reports/hn/1hna | 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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Atom site foot note | 1: CIS PROLINE - PRO 60 |
-Components
#1: Protein | Mass: 25606.422 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / References: UniProt: P28161, glutathione transferase |
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#2: Chemical | ChemComp-GDN / |
#3: Water | ChemComp-HOH / |
Nonpolymer details | ALTHOUGH CRYSTALS WERE GROWN IN THE PRESENCE OF GLUTATHIONE S-(2,4 DINITROBENZENE), ONLY THE ...ALTHOUGH CRYSTALS WERE GROWN IN THE PRESENCE OF GLUTATHION |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.33 Å3/Da / Density % sol: 47.3 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 18 ℃ / Method: vapor diffusion, hanging drop / PH range low: 7.4 / PH range high: 6.8 | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 1.85 Å / Num. obs: 20184 / % possible obs: 97 % / Redundancy: 5.8 % / Rmerge(I) obs: 0.005 / Biso Wilson estimate: 11.22 Å2 / Num. measured all: 28080 |
Reflection shell | *PLUS Mean I/σ(I) obs: 6.6 |
-Processing
Software |
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Refinement | Rfactor Rwork: 0.226 / Rfactor obs: 0.226 / Highest resolution: 1.85 Å Details: THE ELECTRON DENSITY FOR RESIDUES 203 - 217 IS POORLY DEFINED. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 1.85 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 10 Å / Num. reflection all: 20025 / Num. reflection obs: 19682 / σ(F): 2 / Rfactor obs: 0.226 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 1.3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | *PLUS Highest resolution: 1.85 Å / Lowest resolution: 1.92 Å / Total num. of bins used: 10 / Num. reflection obs: 1620 / Rfactor obs: 34.6 |