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''' | ==The structure of a deoxygenated 400 kda hemoglobin provides a more accurate description of the cooperative mechanism of giant hemoglobins: MG bound form== | ||
<StructureSection load='3wcw' size='340' side='right' caption='[[3wcw]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3wcw]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Lamellibrachia_satsuma Lamellibrachia satsuma]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WCW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WCW FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3wct|3wct]], [[3wcu|3wcu]], [[3wcv|3wcv]]</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3wcw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wcw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wcw RCSB], [http://www.ebi.ac.uk/pdbsum/3wcw PDBsum]</span></td></tr> | |||
<table> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Lamellibrachia satsuma]] | |||
[[Category: Fukumori, Y.]] | |||
[[Category: Hasegawa, T.]] | |||
[[Category: Imai, K.]] | |||
[[Category: Kita, A.]] | |||
[[Category: Maruyama, T.]] | |||
[[Category: Miki, K.]] | |||
[[Category: Nakagawa, T.]] | |||
[[Category: Numoto, N.]] | |||
[[Category: Ohara, R.]] | |||
[[Category: Yoshida, T.]] | |||
[[Category: Blood]] | |||
[[Category: Globin fold]] | |||
[[Category: Oxygen binding]] | |||
[[Category: Oxygen transport]] |
Revision as of 08:10, 4 June 2014
The structure of a deoxygenated 400 kda hemoglobin provides a more accurate description of the cooperative mechanism of giant hemoglobins: MG bound formThe structure of a deoxygenated 400 kda hemoglobin provides a more accurate description of the cooperative mechanism of giant hemoglobins: MG bound form
Structural highlights
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