3wcu
From Proteopedia
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| ==The structure of a deoxygenated 400 kda hemoglobin provides a more accurate description of the cooperative mechanism of giant hemoglobins: Deoxygenated form== | ==The structure of a deoxygenated 400 kda hemoglobin provides a more accurate description of the cooperative mechanism of giant hemoglobins: Deoxygenated form== | ||
| - | <StructureSection load='3wcu' size='340' side='right' caption='[[3wcu]], [[Resolution|resolution]] 2.90Å' scene=''> | + | <StructureSection load='3wcu' size='340' side='right'caption='[[3wcu]], [[Resolution|resolution]] 2.90Å' scene=''> | 
| == Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3wcu]] is a 8 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3wcu]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Lamellibrachia_satsuma Lamellibrachia satsuma]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WCU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WCU 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= | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> | 
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3wcu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wcu OCA], [https://pdbe.org/3wcu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wcu RCSB], [https://www.ebi.ac.uk/pdbsum/3wcu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wcu ProSAT]</span></td></tr> | 
| - | <table> | + | </table> | 
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/S0BCU7_LAMSA S0BCU7_LAMSA]  | ||
| <div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| == Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| </div> | </div> | ||
| + | <div class="pdbe-citations 3wcu" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Hemoglobin 3D structures|Hemoglobin 3D structures]] | ||
| == References == | == References == | ||
| <references/> | <references/> | ||
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| </StructureSection> | </StructureSection> | ||
| [[Category: Lamellibrachia satsuma]] | [[Category: Lamellibrachia satsuma]] | ||
| - | [[Category: Fukumori | + | [[Category: Large Structures]] | 
| - | [[Category: Hasegawa | + | [[Category: Fukumori Y]] | 
| - | [[Category: Imai | + | [[Category: Hasegawa T]] | 
| - | [[Category: Kita | + | [[Category: Imai K]] | 
| - | [[Category: Maruyama | + | [[Category: Kita A]] | 
| - | [[Category: Miki | + | [[Category: Maruyama T]] | 
| - | [[Category: Nakagawa | + | [[Category: Miki K]] | 
| - | [[Category: Numoto | + | [[Category: Nakagawa T]] | 
| - | [[Category: Ohara | + | [[Category: Numoto N]] | 
| - | [[Category: Yoshida | + | [[Category: Ohara R]] | 
| - | + | [[Category: Yoshida T]] | |
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Current revision
The structure of a deoxygenated 400 kda hemoglobin provides a more accurate description of the cooperative mechanism of giant hemoglobins: Deoxygenated form
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Categories: Lamellibrachia satsuma | Large Structures | Fukumori Y | Hasegawa T | Imai K | Kita A | Maruyama T | Miki K | Nakagawa T | Numoto N | Ohara R | Yoshida T
