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1mbc
From Proteopedia
(Difference between revisions)
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==X-RAY STRUCTURE AND REFINEMENT OF CARBON-MONOXY (FE II)-MYOGLOBIN AT 1.5 ANGSTROMS RESOLUTION== | ==X-RAY STRUCTURE AND REFINEMENT OF CARBON-MONOXY (FE II)-MYOGLOBIN AT 1.5 ANGSTROMS RESOLUTION== | ||
| - | <StructureSection load='1mbc' size='340' side='right' caption='[[1mbc]], [[Resolution|resolution]] 1.50Å' scene=''> | + | <StructureSection load='1mbc' size='340' side='right'caption='[[1mbc]], [[Resolution|resolution]] 1.50Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1mbc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Phycd Phycd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MBC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MBC FirstGlance]. <br> | <table><tr><td colspan='2'>[[1mbc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Phycd Phycd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MBC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MBC FirstGlance]. <br> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1mbc" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1mbc" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Myoglobin 3D structures|Myoglobin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Phycd]] | [[Category: Phycd]] | ||
[[Category: Kuriyan, J]] | [[Category: Kuriyan, J]] | ||
[[Category: Petsko, G A]] | [[Category: Petsko, G A]] | ||
[[Category: Oxygen storage]] | [[Category: Oxygen storage]] | ||
Revision as of 12:16, 13 November 2019
X-RAY STRUCTURE AND REFINEMENT OF CARBON-MONOXY (FE II)-MYOGLOBIN AT 1.5 ANGSTROMS RESOLUTION
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