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- PDB-1mrj: STUDIES ON CRYSTAL STRUCTURES ACTIVE CENTER GEOMETRY AND DEPURINE... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1mrj | ||||||
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Title | STUDIES ON CRYSTAL STRUCTURES ACTIVE CENTER GEOMETRY AND DEPURINE MECHANISM OF TWO RIBOSOME-INACTIVATING PROTEINS | ||||||
![]() | ALPHA-TRICHOSANTHIN | ||||||
![]() | RIBOSOME-INACTIVATING PROTEIN | ||||||
Function / homology | ![]() regulation of defense response to virus / rRNA N-glycosylase / rRNA N-glycosylase activity / defense response / toxin activity / negative regulation of translation Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Huang, Q. / Liu, S. / Tang, Y. / Jin, S. / Wang, Y. | ||||||
![]() | ![]() Title: Studies on crystal structures, active-centre geometry and depurinating mechanism of two ribosome-inactivating proteins. Authors: Huang, Q. / Liu, S. / Tang, Y. / Jin, S. / Wang, Y. #1: ![]() Title: Active Center Geometry and Depurine Mechanism of Two Ribosome-Inactivating Proteins Authors: Tang, Y. / Huang, Q. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 76.4 KB | Display | ![]() |
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PDB format | ![]() | 57.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 27166.770 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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#2: Chemical | ChemComp-ADN / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.14 Å3/Da / Density % sol: 42.51 % | ||||||||||||||||||
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Crystal grow | *PLUS pH: 6.1 / Method: vapor diffusion, hanging drop | ||||||||||||||||||
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 Num. obs: 21538 / % possible obs: 66.9 % / Rmerge(I) obs: 0.069 |
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Processing
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Refinement | Resolution: 1.6→7 Å / σ(F): 1 /
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Refinement step | Cycle: LAST / Resolution: 1.6→7 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.173 / Rfactor Rwork: 0.173 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 1.2 |