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Open data
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Basic information
Entry | Database: PDB / ID: 1eog | ||||||
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Title | CRYSTAL STRUCTURE OF PI CLASS GLUTATHIONE TRANSFERASE | ||||||
![]() | GLUTATHIONE S-TRANSFERASE | ||||||
![]() | TRANSFERASE / glutathione transferase / helix capping mutant (S149A) | ||||||
Function / homology | ![]() S-nitrosoglutathione binding / nitric oxide storage / negative regulation of smooth muscle cell chemotaxis / negative regulation of leukocyte proliferation / TRAF2-GSTP1 complex / dinitrosyl-iron complex binding / common myeloid progenitor cell proliferation / cellular response to cell-matrix adhesion / hepoxilin biosynthetic process / glutathione derivative biosynthetic process ...S-nitrosoglutathione binding / nitric oxide storage / negative regulation of smooth muscle cell chemotaxis / negative regulation of leukocyte proliferation / TRAF2-GSTP1 complex / dinitrosyl-iron complex binding / common myeloid progenitor cell proliferation / cellular response to cell-matrix adhesion / hepoxilin biosynthetic process / glutathione derivative biosynthetic process / response to L-ascorbic acid / linoleic acid metabolic process / Glutathione conjugation / negative regulation of monocyte chemotactic protein-1 production / nitric oxide binding / JUN kinase binding / glutathione peroxidase activity / Paracetamol ADME / oligodendrocyte development / negative regulation of stress-activated MAPK cascade / negative regulation of JNK cascade / prostaglandin metabolic process / negative regulation of interleukin-1 beta production / cellular response to glucocorticoid stimulus / regulation of stress-activated MAPK cascade / Detoxification of Reactive Oxygen Species / negative regulation of acute inflammatory response / glutathione transferase / negative regulation of vascular associated smooth muscle cell proliferation / glutathione transferase activity / negative regulation of tumor necrosis factor production / protein serine/threonine kinase inhibitor activity / animal organ regeneration / negative regulation of tumor necrosis factor-mediated signaling pathway / response to amino acid / toxic substance binding / regulation of ERK1 and ERK2 cascade / negative regulation of MAPK cascade / negative regulation of fibroblast proliferation / negative regulation of canonical NF-kappaB signal transduction / glutathione metabolic process / xenobiotic metabolic process / cellular response to epidermal growth factor stimulus / positive regulation of superoxide anion generation / fatty acid binding / central nervous system development / response to reactive oxygen species / negative regulation of extrinsic apoptotic signaling pathway / negative regulation of ERK1 and ERK2 cascade / cellular response to insulin stimulus / response to estradiol / cellular response to lipopolysaccharide / response to ethanol / secretory granule lumen / vesicle / ficolin-1-rich granule lumen / Neutrophil degranulation / negative regulation of apoptotic process / negative regulation of transcription by RNA polymerase II / mitochondrion / extracellular space / extracellular exosome / extracellular region / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Rossjohn, J. / McKinstry, W.J. / Oakley, A.J. / Parker, M.W. / Stenberg, G. / Mannervik, B. / Dragani, B. / Cocco, R. / Aceto, A. | ||||||
![]() | ![]() Title: Structures of thermolabile mutants of human glutathione transferase P1-1. Authors: Rossjohn, J. / McKinstry, W.J. / Oakley, A.J. / Parker, M.W. / Stenberg, G. / Mannervik, B. / Dragani, B. / Cocco, R. / Aceto, 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 | ![]() | 90.7 KB | Display | ![]() |
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PDB format | ![]() | 70.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 431.8 KB | Display | ![]() |
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Full document | ![]() | 439.5 KB | Display | |
Data in XML | ![]() | 17.6 KB | Display | |
Data in CIF | ![]() | 24.2 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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Components
#1: Protein | Mass: 23133.455 Da / Num. of mol.: 2 / Mutation: S149A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.68 Å3/Da / Density % sol: 54.1 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 25% ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 20K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 22 ℃ / pH: 7 | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: AREA DETECTOR / Date: Aug 1, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→50 Å / Num. all: 26251 / Num. obs: 23250 |
Reflection | *PLUS % possible obs: 91.6 % / Redundancy: 1.8 % / Num. measured all: 48527 / Rmerge(I) obs: 0.08 |
Reflection shell | *PLUS Rmerge(I) obs: 0.361 / Mean I/σ(I) obs: 2 |
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Processing
Software | Name: CNS / Classification: refinement | ||||||||||||||||||||||||
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Refinement | Resolution: 2.1→50 Å / σ(F): 0
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Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2.1→50 Å
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Refinement | *PLUS Rfactor Rfree: 0.238 / Rfactor Rwork: 0.204 | ||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||
Refine LS restraints | *PLUS
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