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- PDB-1gp1: THE REFINED STRUCTURE OF THE SELENOENZYME GLUTATHIONE PEROXIDASE ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1gp1 | ||||||||||||
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Title | THE REFINED STRUCTURE OF THE SELENOENZYME GLUTATHIONE PEROXIDASE AT 0.2-NM RESOLUTION | ||||||||||||
![]() | GLUTATHIONE PEROXIDASE | ||||||||||||
![]() | OXIDOREDUCTASE(H2O2(A)) | ||||||||||||
Function / homology | ![]() positive regulation of supramolecular fiber organization / endothelial cell development / phospholipid-hydroperoxide glutathione peroxidase activity / response to symbiotic bacterium / regulation of mammary gland epithelial cell proliferation / glutathione peroxidase / Lewy body / protein oxidation / lipoxygenase pathway / blood vessel endothelial cell migration ...positive regulation of supramolecular fiber organization / endothelial cell development / phospholipid-hydroperoxide glutathione peroxidase activity / response to symbiotic bacterium / regulation of mammary gland epithelial cell proliferation / glutathione peroxidase / Lewy body / protein oxidation / lipoxygenase pathway / blood vessel endothelial cell migration / arachidonic acid metabolic process / skeletal muscle tissue regeneration / response to selenium ion / UV protection / angiogenesis involved in wound healing / glutathione peroxidase activity / response to hydroperoxide / myoblast proliferation / biological process involved in interaction with symbiont / temperature homeostasis / triglyceride metabolic process / heart contraction / fat cell differentiation / negative regulation of release of cytochrome c from mitochondria / skeletal muscle fiber development / epigenetic regulation of gene expression / negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / regulation of proteasomal protein catabolic process / negative regulation of extrinsic apoptotic signaling pathway via death domain receptors / negative regulation of inflammatory response to antigenic stimulus / glutathione metabolic process / cell redox homeostasis / hydrogen peroxide catabolic process / response to gamma radiation / sensory perception of sound / negative regulation of cysteine-type endopeptidase activity involved in apoptotic process / response to hydrogen peroxide / SH3 domain binding / peroxidase activity / vasodilation / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / response to xenobiotic stimulus / mitochondrion / cytosol Similarity search - Function | ||||||||||||
Biological species | ![]() ![]() | ||||||||||||
Method | ![]() | ||||||||||||
![]() | Epp, O. / Ladenstein, R. | ||||||||||||
![]() | ![]() Title: The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution. Authors: Epp, O. / Ladenstein, R. / Wendel, A. #1: ![]() Title: Structure Analysis and Molecular Model of the Selenoenzyme Glutathione Peroxidase at 2.8 Angstroms Resolution Authors: Ladenstein, R. / Epp, O. / Bartels, K. / Jones, A. / Huber, R. / Wendel, A. #2: ![]() Title: The Amino-Acid Sequence of Bovine Glutathione Peroxidase Authors: Guenzler, W.A. / Steffens, G.J. / Grossmann, A. / Kim, S.-M.A. / Oetting, F. / Wendel, A. / Flohe, L. | ||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 82.2 KB | Display | ![]() |
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PDB format | ![]() | 65.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 430.5 KB | Display | ![]() |
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Full document | ![]() | 437.2 KB | Display | |
Data in XML | ![]() | 17.7 KB | Display | |
Data in CIF | ![]() | 24.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar 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: SEE REMARK 7. / 2: RESIDUES 97 AND 150 OF EACH CHAIN ARE CIS PROLINES. / 3: SEE REMARK 6. | ||||||||
Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.131858, -0.010348, 0.991227), Vector: |
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Components
#1: Protein | Mass: 21965.893 Da / Num. of mol.: 2 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: 3.24 Å3/Da / Density % sol: 61.99 % | ||||||||||||||||||
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Crystal grow | *PLUS pH: 7.2 / Method: microdialysis | ||||||||||||||||||
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: 2 Å / Num. obs: 26564 / % possible obs: 71 % / Num. measured all: 93223 / Rmerge(I) obs: 0.101 |
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Processing
Software | Name: EREF / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Resolution: 2→6 Å / Rfactor Rwork: 0.171 Details: AN OCCUPANCY OF 0.0 INDICATES THAT NO SIGNIFICANT ELECTRON DENSITY WAS FOUND IN THE FINAL FOURIER MAP. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→6 Å
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Refine LS restraints |
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Refinement | *PLUS Num. reflection obs: 24798 / Rfactor obs: 0.171 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |