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- PDB-1h5a: STRUCTURE OF FERRIC HORSERADISH PEROXIDASE C1A IN COMPLEX WITH ACETATE -
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Open data
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Basic information
Entry | Database: PDB / ID: 1h5a | ||||||
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Title | STRUCTURE OF FERRIC HORSERADISH PEROXIDASE C1A IN COMPLEX WITH ACETATE | ||||||
![]() | PEROXIDASE C1A | ||||||
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Function / homology | ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Berglund, G.I. / Carlsson, G.H. / Hajdu, J. / Smith, A.T. / Szoke, H. / Henriksen, A. | ||||||
![]() | ![]() Title: The Catalytic Pathway of Horseradish Peroxidase at High Resolution Authors: Berglund, G.I. / Carlsson, G.H. / Smith, A.T. / Szoke, H. / Henriksen, A. / Hajdu, J. #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: 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. #3: Journal: J.Biol.Chem. / Year: 1990 Title: Expression of a Synthetic Gene for Horseradish Peroxidase C in Escherichia Coli and Folding and Activation of the Recombinant Enzyme with Ca2+ and Heme Authors: Smith, A.T. / Santama, N. / Dacey, S. / Edwards, M. / Bray, R.C. / Thorneley, R.N. / Burke, J.F. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 81.7 KB | Display | ![]() |
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PDB format | ![]() | 64.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1h55C ![]() 1h57C ![]() 1h58C ![]() 1h5cC ![]() 1h5dC ![]() 1h5eC ![]() 1h5fC ![]() 1h5gC ![]() 1h5hC ![]() 1h5iC ![]() 1h5jC ![]() 1h5kC ![]() 1h5lC ![]() 1h5mC ![]() 1hchC C: citing same article ( |
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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: 33948.141 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: AN ACETATE ION IS BOUND IN THE ACTIVE SITE / Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() | ||||||
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#2: Chemical | ChemComp-HEM / ![]() | ||||||
#3: Chemical | #4: Chemical | ![]() #5: Water | ChemComp-HOH / | ![]() Sequence details | THE SWS ENTRY INCLUDES N-TERM AND C-TERM SIGNAL PEPTIDES. | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.25 Å3/Da / Density % sol: 45.3 % Description: STARTING MODEL FOR RIGID-BODY REFINEMENT WAS PDB ENTRY 7ATJ |
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Crystal grow![]() | pH: 6.5 Details: 20% (W/V) 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: CCD / Date: Feb 15, 1999 / Details: MULTILAYER |
Radiation | Monochromator: DIAMOND (111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.6→19.7 Å / Num. obs: 42167 / % possible obs: 97.7 % / Redundancy: 4.36 % / Biso Wilson estimate: 17.6 Å2 / Rmerge(I) obs: 0.058 / Net I/σ(I): 18.2 |
Reflection shell | Resolution: 1.6→1.64 Å / Rmerge(I) obs: 0.203 / Mean I/σ(I) obs: 6.8 / % possible all: 93.9 |
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Processing
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Refinement | Method to determine structure![]() Details: SER 306 WAS THE LAST RESIDUE SEEN IN THE ELECTRON DENSITY MAP THE FOLLOWING RESIDUES HAVE BEEN MODELLED IN DUAL CONFORMATIONS: 15,24,91,151,161,188,219,240, 249,286,296
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 49.644 Å2 / ksol: 0.358411 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 16.7 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.6→19.71 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.6→1.7 Å / Rfactor Rfree error: 0.014 / Total num. of bins used: 6
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Xplor file |
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