3wct
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==The structure of a deoxygenated 400 kda hemoglobin provides a more accurate description of the cooperative mechanism of giant hemoglobins: Oxygenated form== |
| - | + | <StructureSection load='3wct' size='340' side='right' caption='[[3wct]], [[Resolution|resolution]] 2.40Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3wct]] 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=3WCT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WCT FirstGlance]. <br> | |
| - | + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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">[[3wcu|3wcu]], [[3wcv|3wcv]], [[3wcw|3wcw]]</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=3wct FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wct OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wct RCSB], [http://www.ebi.ac.uk/pdbsum/3wct 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 05:10, 4 June 2014
The structure of a deoxygenated 400 kda hemoglobin provides a more accurate description of the cooperative mechanism of giant hemoglobins: Oxygenated form
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