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A NOVEL SITE-DIRECTED MUTANT OF MYOGLOBIN WITH AN UNUSUALLY HIGH O2 AFFINITY AND LOW AUTOOXIDATION RATE
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jpquast
Created on Thu, 2020-11-26 04:30, last updated on Thu, 2020-11-26 04:30
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General Information
This Model was autogenerated from the
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tool.
Model ID
3DPX-015169
Category
Proteins, Macromolecules and Viruses
Keyword(s)
OXYGEN STORAGE
Protein Data Bank ID
1MOA
Experimental Method
X-RAY DIFFRACTION
Model Details
Oligomeric Details
monomeric
R-Factor
0.1546000
Scattering Type
x-ray
Attribution
PubMed ID
1 629 229
Citation Title
A novel site-directed mutant of myoglobin with an unusually high O2 affinity and low autooxidation rate.
Citation Year
1992
STL/VRML Files
PDB-1MOA-ribbon-secondary.wrl
PDB-1MOA-ribbon-rainbow.wrl
PDB-1MOA-ribbon-bychain.wrl
PDB-1MOA-ribbon.stl
PDB-1MOA-surf-bychain.wrl
PDB-1MOA-surf-hydropathy.wrl
PDB-1MOA-surf-coulombic.wrl
PDB-1MOA-surf.stl
PDB-1MOA.zip
X3D Files
PDB-1MOA-ribbon-secondary.x3d
PDB-1MOA-ribbon-rainbow.x3d
PDB-1MOA-ribbon-bychain.x3d
PDB-1MOA-ribbon.x3d
PDB-1MOA-surf-bychain.x3d
PDB-1MOA-surf-hydropathy.x3d
PDB-1MOA-surf-coulombic.x3d
PDB-1MOA-surf.x3d
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