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- PDB-2pqi: Crystal structure of active ribosome inactivating protein from ma... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2pqi | ||||||
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Title | Crystal structure of active ribosome inactivating protein from maize (b-32) | ||||||
![]() | Ribosome-inactivating protein 3 | ||||||
![]() | HYDROLASE / MOD / ribosome inactivating protein / maize / Plant defense / Protein synthesis inhibitor / Toxin | ||||||
Function / homology | ![]() rRNA N-glycosylase / rRNA N-glycosylase activity / defense response / toxin activity / negative regulation of translation / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Mak, A.N.S. / Wong, Y.T. / Young, J.A. / Cha, S.S. / Sze, K.H. / Au, S.W.N. / Wong, K.B. / Shaw, P.C. | ||||||
![]() | ![]() Title: Structure-function study of maize ribosome-inactivating protein: implications for the internal inactivation region and the sole glutamate in the active site. Authors: Mak, A.N. / Wong, Y.T. / An, Y.J. / Cha, S.S. / Sze, K.H. / Au, S.W. / Wong, K.B. / Shaw, P.C. #1: Journal: J.Biol.Chem. / Year: 1991 Title: Characterization and molecular cloning of a proenzyme form of a ribosome-inactivating protein from maize. Novel mechanism of proenzyme activation by proteolytic removal of a 2.8-kilodalton ...Title: Characterization and molecular cloning of a proenzyme form of a ribosome-inactivating protein from maize. Novel mechanism of proenzyme activation by proteolytic removal of a 2.8-kilodalton internal peptide segment. Authors: Walsh, T.A. / Morgan, A.E. / Hey, T.D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 146.1 KB | Display | ![]() |
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PDB format | ![]() | 114.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 449.8 KB | Display | ![]() |
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Full document | ![]() | 484.1 KB | Display | |
Data in XML | ![]() | 30.5 KB | Display | |
Data in CIF | ![]() | 40.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2pqgSC ![]() 2pqjC S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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3 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 27305.551 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P25891, UniProt: P28522*PLUS, rRNA N-glycosylase #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.1 Å3/Da / Density % sol: 41.52 % |
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Crystal grow | Temperature: 299 K / Method: vapor diffusion, sitting drop / pH: 8.5 Details: 0.2 M Sodium acetate tri-hydrate, 0.1 M Tris-HCl pH 8.5, 30% PEG 4000, VAPOR DIFFUSION, SITTING DROP, temperature 299K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Nov 1, 2006 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54178 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→20 Å / Num. all: 21654 / Num. obs: 21654 / % possible obs: 93.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 2.4 % / Rmerge(I) obs: 0.031 / Net I/σ(I): 22.2 |
Reflection shell | Resolution: 2.5→2.59 Å / Redundancy: 2 % / Rmerge(I) obs: 0.153 / Mean I/σ(I) obs: 4.1 / % possible all: 90.1 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB entry 2PQG Resolution: 2.5→20 Å / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.5→20 Å
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Refine LS restraints |
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