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Open data
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Basic information
Entry | Database: PDB / ID: 1gwo | ||||||
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Title | Recombinant horseradish peroxidase C1A ALA170GLN | ||||||
![]() | PEROXIDASE C1A | ||||||
![]() | OXIDOREDUCTASE / PEROXIDASE | ||||||
Function / homology | ![]() lactoperoxidase activity / peroxidase / vacuole / hydrogen peroxide catabolic process / response to oxidative stress / heme binding / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Henriksen, A. / Brissett, N. / Gajhede, M. | ||||||
![]() | ![]() Title: Hrpc Heme Crevice Architecture Authors: Henriksen, A. / Brissett, N. / Meno, K. / Mirza, O. / Gajhede, M. #1: ![]() Title: The Structures of the Horseradish Peroxidase C-Ferulic Acid Complex and the Ternary Complex with Cyanide Suggest How Peroxidases Oxidize Small Phenolic Substrates Authors: Henriksen, A. / Smith, A.T. / Gajhede, M. #2: ![]() Title: Structural Interactions between Horseradish Peroxidase C and the Substrate Benzhydroxamic Acid Determined by X-Ray Crystallography Authors: Henriksen, A. / Schuller, D.J. / Meno, K. / Welinder, K.G. / Smith, A.T. / Gajhede, M. #3: ![]() Title: Crystal Structure of Horseradish Peroxidase C at 2.15 A Resolution Authors: Gajhede, M. / Schuller, D.J. / Henriksen, A. / Smith, A.T. / Poulos, T.L. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 86.5 KB | Display | ![]() |
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PDB format | ![]() | 62.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 794.8 KB | Display | ![]() |
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Full document | ![]() | 796.7 KB | Display | |
Data in XML | ![]() | 17.7 KB | Display | |
Data in CIF | ![]() | 27.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1gw2C ![]() 1gwtC ![]() 1gwuC ![]() 1gx2C ![]() 7atjS C: citing same article ( S: Starting model for refinement |
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Similar 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: 34136.391 Da / Num. of mol.: 1 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||||||
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#2: Chemical | ChemComp-HEM / | ||||||
#3: Chemical | #4: Chemical | ChemComp-ACT / | #5: Water | ChemComp-HOH / | Compound details | ENGINEERED | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.35 Å3/Da / Density % sol: 47 % |
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Crystal grow | pH: 6.5 Details: 16% PEG 4000, 0.2 M CALCIUM ACETATE, 0.1 M CACODYLATE BUFFER PH 6.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jun 15, 2000 / Details: MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.07→44.32 Å / Num. obs: 18682 / % possible obs: 91.6 % / Observed criterion σ(I): 0 / Redundancy: 9.9 % / Biso Wilson estimate: 10.2 Å2 / Rmerge(I) obs: 0.105 |
Reflection shell | Resolution: 2.07→2.14 Å / Rmerge(I) obs: 0.301 / % possible all: 82.7 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 7ATJ Resolution: 2.07→44.32 Å / Rfactor Rfree error: 0.005 / Data cutoff high absF: 247761.96 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: MLF
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 67.6716 Å2 / ksol: 0.372831 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 18.7 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.07→44.32 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.07→2.2 Å / Rfactor Rfree error: 0.016 / Total num. of bins used: 6
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