+Open data
-Basic information
Entry | Database: PDB / ID: 1mn2 | |||||||||
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Title | MANGANESE PEROXIDASE SUBSTRATE BINDING SITE MUTANT E35Q, D179N | |||||||||
Components | MANGANESE PEROXIDASE | |||||||||
Keywords | PEROXIDASE / DONOR: H2O2 OXIDOREDUCTASE / HEME ENZYME | |||||||||
Function / homology | Function and homology information manganese peroxidase / manganese peroxidase activity / lignin catabolic process / response to reactive oxygen species / hydrogen peroxide catabolic process / cellular response to oxidative stress / heme binding / extracellular region / metal ion binding Similarity search - Function | |||||||||
Biological species | Phanerochaete chrysosporium (fungus) | |||||||||
Method | X-RAY DIFFRACTION / DIFFERENCE FOURIER / Resolution: 2 Å | |||||||||
Authors | Sundaramoorthy, M. / Poulos, T.L. | |||||||||
Citation | Journal: J.Biol.Chem. / Year: 1997 Title: Crystal structures of substrate binding site mutants of manganese peroxidase. Authors: Sundaramoorthy, M. / Kishi, K. / Gold, M.H. / Poulos, T.L. #1: Journal: J.Biol.Chem. / Year: 1994 Title: The Crystal Structure of Manganese Peroxidase from Phanerochaete Chrysosporium at 2.06-A Resolution Authors: Sundaramoorthy, M. / Kishi, K. / Gold, M.H. / Poulos, T.L. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1mn2.cif.gz | 82.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1mn2.ent.gz | 64.3 KB | Display | PDB format |
PDBx/mmJSON format | 1mn2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1mn2_validation.pdf.gz | 1.1 MB | Display | wwPDB validaton report |
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Full document | 1mn2_full_validation.pdf.gz | 1.1 MB | Display | |
Data in XML | 1mn2_validation.xml.gz | 17.7 KB | Display | |
Data in CIF | 1mn2_validation.cif.gz | 25.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mn/1mn2 ftp://data.pdbj.org/pub/pdb/validation_reports/mn/1mn2 | HTTPS FTP |
-Related 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: 37481.000 Da / Num. of mol.: 1 / Mutation: E35Q, D179N Source method: isolated from a genetically manipulated source Source: (gene. exp.) Phanerochaete chrysosporium (fungus) / Strain: OGC101 / Description: WOOD-ROTTING FUNGUS / Cellular location: EXTRACELLULAR / Gene: MNP1 / Variant: OGC107-1 / Plasmid: PUC18 / Gene (production host): MNP1 / Production host: Phanerochaete chrysosporium (fungus) / Strain (production host): OGC107-1 (ADE1) / Variant (production host): D179N-6 / References: UniProt: Q02567, manganese peroxidase | ||||
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#2: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source | ||||
#3: Chemical | #4: Chemical | ChemComp-HEM / | #5: 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: 2.66 Å3/Da / Density % sol: 53.73 % Description: NATIVE STRUCTURE (CODE :1MNP) WAS USED AS THE STARTING MODEL | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 6.5 Details: 30% PEG 8000, 0.2 M AMMONIUM SULFATE, 0.1 M SODIUM CACODYLATE BUFFER, PH 6.5 | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 295 K |
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Diffraction source | Source: ROTATING ANODE / Type: SIEMENS / Wavelength: 1.5418 |
Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: Oct 3, 1995 / Details: SUPPER MIRRORS |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Highest resolution: 2 Å / Num. obs: 27424 / % possible obs: 98 % / Observed criterion σ(I): 1 / Redundancy: 2.9 % / Rsym value: 0.106 / Net I/σ(I): 13.6 |
Reflection shell | Resolution: 2→2.2 Å / Redundancy: 2.1 % / Mean I/σ(I) obs: 1.9 / Rsym value: 0.294 / % possible all: 98 |
Reflection | *PLUS Num. measured all: 91040 / Rmerge(I) obs: 0.1061 |
-Processing
Software |
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Refinement | Method to determine structure: DIFFERENCE FOURIER / Resolution: 2→8 Å / σ(F): 2 /
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Refinement step | Cycle: LAST / Resolution: 2→8 Å
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Refine LS restraints |
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Xplor file |
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Software | *PLUS Name: X-PLOR / Version: 3.8 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Num. reflection all: 25117 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |