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Yorodumi- PDB-1cck: ALTERING SUBSTRATE SPECIFICITY OF CYTOCHROME C PEROXIDASE TOWARDS... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1cck | ||||||
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Title | ALTERING SUBSTRATE SPECIFICITY OF CYTOCHROME C PEROXIDASE TOWARDS A SMALL MOLECULAR SUBSTRATE PEROXIDASE BY SUBSTITUTING TYROSINE FOR PHE 202 | ||||||
Components | CYTOCHROME C PEROXIDASE | ||||||
Keywords | OXIDOREDUCTASE / PEROXIDASE | ||||||
Function / homology | Function and homology information cytochrome-c peroxidase / cytochrome-c peroxidase activity / response to reactive oxygen species / hydrogen peroxide catabolic process / peroxidase activity / mitochondrial intermembrane space / cellular response to oxidative stress / mitochondrial matrix / heme binding / mitochondrion / metal ion binding Similarity search - Function | ||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.1 Å | ||||||
Authors | Cao, Y. / Musah, R.A. / Wilcox, S.K. / Goodin, D.B. / Mcree, D.E. | ||||||
Citation | Journal: Biochemistry / Year: 1995 Title: Crystal structure of recombinant pea cytosolic ascorbate peroxidase. Authors: Patterson, W.R. / Poulos, T.L. #1: Journal: Biochemistry / Year: 1996 Title: Altering Substrate Specificity at the Heme Edge of Cytochrome C Peroxidase Authors: Wilcox, S.K. / Jensen, G.M. / Fitzgerald, M.M. / Mcree, D.E. / Goodin, D.B. #2: Journal: Biochemistry / Year: 1993 Title: The Asp-His-Fe Triad of Cytochrome C Peroxidase Controls the Reduction Potential, Electronic Structure, and Coupling of the Tryptophan Free Radical to the Heme Authors: Goodin, D.B. / Mcree, D.E. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1cck.cif.gz | 82.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1cck.ent.gz | 65.1 KB | Display | PDB format |
PDBx/mmJSON format | 1cck.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cc/1cck ftp://data.pdbj.org/pub/pdb/validation_reports/cc/1cck | HTTPS FTP |
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-Related structure data
Related structure data | 1apxC 1ccaS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 33241.938 Da / Num. of mol.: 1 / Mutation: F202Y Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast) Cell line: BL21 / Gene: CCP / Organelle: MITOCHONDRIAMitochondrion / Plasmid: PT7CCP / Species (production host): Escherichia coli / Cellular location (production host): CYTOPLASM / Gene (production host): CCP(MKT) / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: P00431, cytochrome-c peroxidase |
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#2: Chemical | ChemComp-HEM / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.1 Å3/Da / Density % sol: 61 % |
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Crystal grow | Method: dialaysis / Details: DIALYSIS AGAINST DISTILLED WATER, dialaysis |
Crystal grow | *PLUS Method: unknown |
-Data collection
Diffraction | Mean temperature: 290 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RUH2R / Wavelength: 1.5418 |
Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: Jun 1, 1995 / Details: NO |
Radiation | Monochromator: NO / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Highest resolution: 2.1 Å / Num. obs: 23157 / % possible obs: 91.3 % / Observed criterion σ(I): 1.1 / Redundancy: 2.2 % / Biso Wilson estimate: 41.4 Å2 / Rmerge(I) obs: 0.07 / Rsym value: 0.094 / Net I/σ(I): 7.1 |
Reflection shell | Resolution: 2.01→2.09 Å / Redundancy: 1.7 % / Mean I/σ(I) obs: 1 / Rsym value: 0.29 / % possible all: 77.5 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1CCA Resolution: 2.1→5 Å / Data cutoff high absF: 100000 / Data cutoff low absF: 1 /
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Refinement step | Cycle: LAST / Resolution: 2.1→5 Å
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Xplor file |
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Refinement | *PLUS Rfactor obs: 0.184 / Rfactor Rwork: 0.184 | |||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||
Displacement parameters | *PLUS |