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- PDB-1cce: CONSTRUCTION OF A BIS-AQUO HEME ENZYME AND REPLACEMENT WITH EXOGE... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1cce | ||||||
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Title | CONSTRUCTION OF A BIS-AQUO HEME ENZYME AND REPLACEMENT WITH EXOGENOUS LIGAND | ||||||
![]() | CYTOCHROME C PEROXIDASE![]() | ||||||
![]() | OXIDOREDUCTASE(H2O2(A)) | ||||||
Function / homology | ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Mcree, D.E. / Jensen, G.M. / Fitzgerald, M.M. / Siegel, H.A. / Goodin, D.B. | ||||||
![]() | ![]() Title: Construction of a bisaquo heme enzyme and binding by exogenous ligands. Authors: McRee, D.E. / Jensen, G.M. / Fitzgerald, M.M. / Siegel, H.A. / Goodin, D.B. #1: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 85.2 KB | Display | ![]() |
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PDB format | ![]() | 63.7 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: 33144.844 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P00431, ![]() |
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#2: Chemical | ChemComp-HEM / ![]() |
#3: Water | ChemComp-HOH / ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.68 Å3/Da / Density % sol: 54.02 % | |||||||||||||||||||||||||
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Crystal grow![]() | *PLUS Temperature: 4 K / pH: 6 / Method: vapor diffusion, sitting 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 Highest resolution: 2.3 Å / Num. obs: 17907 / % possible obs: 91 % / Num. measured all: 86869 / Rmerge(I) obs: 0.105 |
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Processing
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Refinement | Resolution: 2.3→7 Å / σ(F): 2 /
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Refinement step | Cycle: LAST / Resolution: 2.3→7 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.19 / Rfactor Rwork![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 3.1 |