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- PDB-1beq: INTERACTION BETWEEN PROXIMAL AND DISTALS REGIONS OF CYTOCHROME C ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1beq | ||||||
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Title | INTERACTION BETWEEN PROXIMAL AND DISTALS REGIONS OF CYTOCHROME C PEROXIDASE | ||||||
![]() | CYTOCHROME C PEROXIDASE | ||||||
![]() | PEROXIDASE / OXIDOREDUCTASE | ||||||
Function / homology | ![]() cytochrome-c peroxidase / cytochrome-c peroxidase activity / response to reactive oxygen species / hydrogen peroxide catabolic process / mitochondrial intermembrane space / peroxidase activity / cellular response to oxidative stress / mitochondrial matrix / heme binding / mitochondrion / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Miller, M.A. | ||||||
![]() | ![]() Title: Interaction between Proximal and Distals Regions of Cytochrome C Peroxidase Authors: Miller, M.A. / Han, G.W. / Kraut, J. #1: ![]() Title: A Ligand-Gated, Hinged Loop Rearrangement Opens a Channel to a Buried Artificial Protein Cavity Authors: Fitzgerald, M.M. / Musah, R.A. / Mcree, D.E. / Goodin, D.B. #2: ![]() Title: A Cation Binding Motif Stabilizes the Compound I Radical of Cytochrome C Peroxidase Authors: Miller, M.A. / Han, G.W. / Kraut, J. #3: ![]() Title: X-Ray Structures of Recombinant Yeast Cytochrome C Peroxidase and Three Heme-Cleft Mutants Prepared by Site-Directed Mutagenesis Authors: Wang, J.M. / Mauro, M. / Edwards, S.L. / Oatley, S.J. / Fishel, L.A. / Ashford, V.A. / Xuong, N.H. / Kraut, J. #4: ![]() Title: Yeast Cytochrome C Peroxidase: Mutagenesis and Expression in Escherichia Coli Show Tryptophan-51 is not the Radical Site in Compound I Authors: Fishel, L.A. / Villafranca, J.E. / Mauro, J.M. / Kraut, J. #5: ![]() Title: Crystal Structure of Yeast Cytochrome C Peroxidase Refined at 1.7-A Resolution Authors: Finzel, B.C. / Poulos, T.L. / Kraut, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 78.9 KB | Display | ![]() |
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PDB format | ![]() | 57.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 488 KB | Display | ![]() |
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Full document | ![]() | 500.3 KB | Display | |
Data in XML | ![]() | 9.4 KB | Display | |
Data in CIF | ![]() | 14.2 KB | Display | |
Arichive directory | ![]() ![]() | 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: 33203.887 Da / Num. of mol.: 1 / Mutation: MET ILE ADDED AT N-TERMINUS, W191Y Source method: isolated from a genetically manipulated source Details: COMPLEXED WITH A MES (+) ZWITTERION Source: (gene. exp.) ![]() ![]() Production host: ![]() ![]() |
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#2: Chemical | ChemComp-HEM / |
#3: Chemical | ChemComp-MES / |
#4: Water | ChemComp-HOH / |
Compound details | THE MUTATION DESTABILIZES THE 191 LOOP. IN MES BUFFER, A MOLECULE OF MES BINDS TO THE ENZYME, AND ...THE MUTATION DESTABILIZ |
Sequence details | THIS CYTOCHROME C PEROXIDASE DIFFERS FROM A PREVIOUSLY DEPOSITED STRUCTURE (PROTEIN DATA BANK ENTRY ...THIS CYTOCHROME |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.63 Å3/Da / Density % sol: 53 % |
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Crystal grow | pH: 6 / Details: 30% MPD; 50 MM MES/TRIS, PH 6.0 |
-Data collection
Diffraction | Mean temperature: 273 K |
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Diffraction source | Wavelength: 1.5418 |
Detector | Date: Oct 1, 1997 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Highest resolution: 2.16 Å |
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Processing
Software | Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
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Refinement | Resolution: 2.16→20 Å / Isotropic thermal model: BCORREL / σ(F): 2 / Stereochemistry target values: PROTGEO Details: COORDINATES FOR RESIDUES -1, 0, AND 1 - 3 ARE NOT INCLUDED IN THIS ENTRY BECAUSE THESE RESIDUES COULD NOT BE RESOLVED IN THE FINAL ELECTRON DENSITY MAPS. WATER MOLECULES WITH B-FACTORS ...Details: COORDINATES FOR RESIDUES -1, 0, AND 1 - 3 ARE NOT INCLUDED IN THIS ENTRY BECAUSE THESE RESIDUES COULD NOT BE RESOLVED IN THE FINAL ELECTRON DENSITY MAPS. WATER MOLECULES WITH B-FACTORS GREATER THAN 80 WERE NOT INCLUDED IN THE MODEL.
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Refinement step | Cycle: LAST / Resolution: 2.16→20 Å
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Refine LS restraints |
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