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Yorodumi- PDB-351c: STRUCTURE OF CYTOCHROME C551 FROM P. AERUGINOSA REFINED AT 1.6 AN... -
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Basic information
| Entry | Database: PDB / ID: 351c | |||||||||
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| Title | STRUCTURE OF CYTOCHROME C551 FROM P. AERUGINOSA REFINED AT 1.6 ANGSTROMS RESOLUTION AND COMPARISON OF THE TWO REDOX FORMS | |||||||||
Components | CYTOCHROME C551 | |||||||||
Keywords | ELECTRON TRANSPORT | |||||||||
| Function / homology | Function and homology informationperiplasmic space / electron transfer activity / iron ion binding / heme binding Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | X-RAY DIFFRACTION / Resolution: 1.6 Å | |||||||||
Authors | Matsuura, Y. / Takano, T. / Dickerson, R.E. | |||||||||
Citation | Journal: J.Mol.Biol. / Year: 1982Title: Structure of cytochrome c551 from Pseudomonas aeruginosa refined at 1.6 A resolution and comparison of the two redox forms. Authors: Matsuura, Y. / Takano, T. / Dickerson, R.E. #1: Journal: Proc.Natl.Acad.Sci.USA / Year: 1978Title: Pseudomonas Cytochrome C551 at 2.0 Angstroms Resolution. Enlargement of the Cytochrome C Family Authors: Almassy, R.J. / Dickerson, R.E. #2: Journal: J.Mol.Biol. / Year: 1976Title: The Cytochrome Fold and the Evolution of Bacterial Energy Metabolism Authors: Dickerson, R.E. / Timkovich, R. / Almassy, R.J. | |||||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 351c.cif.gz | 30.6 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb351c.ent.gz | 19.6 KB | Display | PDB format |
| PDBx/mmJSON format | 351c.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 351c_validation.pdf.gz | 797.6 KB | Display | wwPDB validaton report |
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| Full document | 351c_full_validation.pdf.gz | 798.9 KB | Display | |
| Data in XML | 351c_validation.xml.gz | 7.6 KB | Display | |
| Data in CIF | 351c_validation.cif.gz | 9.4 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/51/351c ftp://data.pdbj.org/pub/pdb/validation_reports/51/351c | 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: 8704.892 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() | ||||
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| #2: Chemical | | #3: Water | ChemComp-HOH / | Has protein modification | Y | |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION |
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Sample preparation
| Crystal | Density Matthews: 2.07 Å3/Da / Density % sol: 40.6 % | ||||||||||||||||||||||||
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| Crystal grow | *PLUS Method: microdialysis / PH range low: 5.7 / PH range high: 5.6 | ||||||||||||||||||||||||
| Components of the solutions | *PLUS
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-Data collection
| Reflection | *PLUS Num. obs: 8670 |
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Processing
| Refinement | Highest resolution: 1.6 Å /
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| Refinement step | Cycle: LAST / Highest resolution: 1.6 Å
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| Refinement | *PLUS Rfactor obs: 0.195 | ||||||||||||
| Solvent computation | *PLUS | ||||||||||||
| Displacement parameters | *PLUS |
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