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Yorodumi- PDB-1b4p: CRYSTAL STRUCTURES OF CLASS MU CHIMERIC GST ISOENZYMES M1-2 AND M2-1 -
+Open data
-Basic information
Entry | Database: PDB / ID: 1b4p | ||||||
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Title | CRYSTAL STRUCTURES OF CLASS MU CHIMERIC GST ISOENZYMES M1-2 AND M2-1 | ||||||
Components | PROTEIN (GLUTATHIONE S-TRANSFERASE) | ||||||
Keywords | TRANSFERASE / CHIMERIC GST | ||||||
Function / homology | Function and homology information response to catechin / Glutathione conjugation / nitrobenzene metabolic process / cellular detoxification of nitrogen compound / : / response to genistein / glutathione binding / hepoxilin biosynthetic process / linoleic acid metabolic process / glutathione peroxidase activity ...response to catechin / Glutathione conjugation / nitrobenzene metabolic process / cellular detoxification of nitrogen compound / : / response to genistein / glutathione binding / hepoxilin biosynthetic process / linoleic acid metabolic process / glutathione peroxidase activity / response to metal ion / 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 / xenobiotic catabolic process / regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum / xenobiotic metabolic process / glutathione metabolic process / sarcoplasmic reticulum / fatty acid binding / response to organic cyclic compound / sensory perception of smell / signaling receptor binding / enzyme binding / protein homodimerization activity / protein-containing complex / identical protein binding / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Rattus norvegicus (Norway rat) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.7 Å | ||||||
Authors | Xiao, G. / Chen, J. / Armstrong, R.N. / Gilliland, G.L. | ||||||
Citation | Journal: To be Published Title: Crystal Structures of Class MU Chimeric GST Isoenzymes M1-2 and M2-1 Authors: Xiao, G. / Liu, X. / Ji, X. / Zhang, P. / Johnson, W.W. / Chen, J. / Parsons, J.F. / Stevens, W.J. / Gilliland, G.L. / Armstrong, R.N. #1: Journal: Biochemistry / Year: 1996 Title: First-Sphere and Second-Sphere Electrostatic Effects in the Active Site of a Class Mu Glutathione S-Transferease Authors: Ji, X. / Zhang, P. / Johnson, W.W. / Sesay, M.A. / Dickert, L. / Prasad, S.S. / Ammon, H.L. / Armstrong, R.N. / Gilliland, G.L. #2: Journal: Biochemistry / Year: 1994 Title: Structure and Function of the Xenobiotic Substrate Binding Site of a Glutathione S-Transferease as Revealed by X-Ray Crystallogaphic Anaysis of Product Complexes with the Diastereomers of 9-(S- ...Title: Structure and Function of the Xenobiotic Substrate Binding Site of a Glutathione S-Transferease as Revealed by X-Ray Crystallogaphic Anaysis of Product Complexes with the Diastereomers of 9-(S-Glutathionyl)-10-Hydroxy-9,10- Dihydrophenanthren E Authors: Ji, X. / Zhang, P. / Armstrong, R.N. / Gilliland, G.L. #3: Journal: Biochemistry / Year: 1992 Title: The Three-Dimensional Structure of a Glutathione S-Transferease from the Mu Gene Class. Structural Analysis of the Binary Complex of Isoenzyme 3-3 and Glutathione at 2.2-A Resolution | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1b4p.cif.gz | 68 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1b4p.ent.gz | 49.6 KB | Display | PDB format |
PDBx/mmJSON format | 1b4p.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1b4p_validation.pdf.gz | 1.1 MB | Display | wwPDB validaton report |
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Full document | 1b4p_full_validation.pdf.gz | 1.1 MB | Display | |
Data in XML | 1b4p_validation.xml.gz | 16.3 KB | Display | |
Data in CIF | 1b4p_validation.cif.gz | 23.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/b4/1b4p ftp://data.pdbj.org/pub/pdb/validation_reports/b4/1b4p | HTTPS FTP |
-Related structure data
Related structure data | 1gst 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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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 25740.738 Da / Num. of mol.: 1 / Fragment: COMPLETE PROTEIN Source method: isolated from a genetically manipulated source Details: SUBSTRATE IS (9S, 10S)-9-(S-GLUTATHIONYL)-10-HYDROXY-9.10-DIHYDROPHENANTHRENE Source: (gene. exp.) Rattus norvegicus (Norway rat) / Strain: M5219 Description: THE ENZYME IS A CHIMERIC GST, CONSISTING OF DOMAIN I FROM TYPE M1-1 AND DOMAIN II FROM TYPE M2-2 Gene: CDNA INSERT OF CLONE PGT33MX / Organ: LIVER / Plasmid: PGT33MX / Gene (production host): CDNA INSERT OF CLONE PGT33MX / Production host: Escherichia coli (E. coli) / Strain (production host): M5219 / References: UniProt: P08010, glutathione transferase | ||||||
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#2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | Sequence details | FOR THIS CHIMERIC GST M1-2, THE SEQUENCE IN DOMAIN I IS IDENTICAL TO THAT IN M1-1 AND THE SEQUENCE ...FOR THIS CHIMERIC GST M1-2, THE SEQUENCE IN DOMAIN I IS IDENTICAL TO THAT IN M1-1 AND THE SEQUENCE IN DOMAIN II TO THAT IN M2-2 | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.32 Å3/Da / Density % sol: 47 % |
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Crystal grow | pH: 8 Details: PROTEIN CONC. 10 MG/ML, 25 MM TRIS BUFFER (PH 8.0), 1 MM EDTA, 0.3% OCTYL BETA- D-GLUCOPYRANOSIDE, 2 MM PRODUCT INHIBITOR (GPS) |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: BRUKER / Wavelength: 1.5418 |
Detector | Type: BRUKER / Detector: AREA DETECTOR / Date: Apr 15, 1996 |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→20 Å / Num. obs: 27013 / % possible obs: 98.3 % / Observed criterion σ(I): 0 / Redundancy: 8.6 % / Rsym value: 0.088 / Net I/σ(I): 8.6 |
Reflection shell | Resolution: 1.7→1.81 Å / Redundancy: 36 % / Mean I/σ(I) obs: 1.9 / Rsym value: 0.44 / % possible all: 89.7 |
-Processing
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1GST 1gst Resolution: 1.7→6 Å / σ(F): 2
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Refinement step | Cycle: LAST / Resolution: 1.7→6 Å
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Refine LS restraints |
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