+Open data
-Basic information
Entry | Database: PDB / ID: 1m3j | ||||||
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Title | CRYSTAL form II of perfringolysin O | ||||||
Components | perfringolysin o | ||||||
Keywords | TOXIN / PORE FORMING TOXIN | ||||||
Function / homology | Function and homology information hemolysis in another organism / cholesterol binding / toxin activity / membrane => GO:0016020 / host cell plasma membrane / extracellular region / membrane Similarity search - Function | ||||||
Biological species | Clostridium perfringens (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3 Å | ||||||
Authors | Rossjohn, J. / Parker, M. / Polekhina, G. / Feil, S. / Tweten, R. | ||||||
Citation | Journal: To be Published Title: STRUCTURAL SNAPSHOTS IN THE MOLECULAR MECHANISM OF PFO REVEALED Authors: ROSSJOHN, J. / PARKER, M. / POLEKHINA, G. / FEIL, S. / TWETEN, R. | ||||||
History |
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Remark 999 | SEQUENCE ACCORDING TO THE AUTHOR, THIS REPRESENTS AN ERROR IN THE INITIAL PROTEIN SEQUENCE ...SEQUENCE ACCORDING TO THE AUTHOR, THIS REPRESENTS AN ERROR IN THE INITIAL PROTEIN SEQUENCE DETERMINATION. REFER TO PDB ENTRY 1PFO. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1m3j.cif.gz | 192.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1m3j.ent.gz | 153 KB | Display | PDB format |
PDBx/mmJSON format | 1m3j.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/m3/1m3j ftp://data.pdbj.org/pub/pdb/validation_reports/m3/1m3j | HTTPS FTP |
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-Related structure data
Related structure data | 1pfoS 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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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 52571.516 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Clostridium perfringens (bacteria) / Production host: Escherichia coli (E. coli) / References: UniProt: P19995, UniProt: P0C2E9*PLUS #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 4 Å3/Da / Density % sol: 69.25 % |
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X11 / Wavelength: 1 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 3→20 Å / Num. all: 24516 / Num. obs: 24516 / % possible obs: 70.5 % / Observed criterion σ(F): -5 / Observed criterion σ(I): -5 / Redundancy: 1.8 % / Rmerge(I) obs: 0.151 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: pdb entry 1pfo Resolution: 3→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: 3→20 Å
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