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3a0g
From Proteopedia
(Difference between revisions)
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==Crystal structure analysis of guinea pig oxyhemoglobin at 2.5 angstroms resolution== | ==Crystal structure analysis of guinea pig oxyhemoglobin at 2.5 angstroms resolution== | ||
<StructureSection load='3a0g' size='340' side='right' caption='[[3a0g]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='3a0g' size='340' side='right' caption='[[3a0g]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hho|1hho]], [[1a4f|1a4f]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hho|1hho]], [[1a4f|1a4f]]</td></tr> | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3a0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a0g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3a0g RCSB], [http://www.ebi.ac.uk/pdbsum/3a0g PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3a0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a0g OCA], [http://pdbe.org/3a0g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3a0g RCSB], [http://www.ebi.ac.uk/pdbsum/3a0g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3a0g ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| - | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3a0g ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
Revision as of 11:25, 4 August 2016
Crystal structure analysis of guinea pig oxyhemoglobin at 2.5 angstroms resolution
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Categories: Cavia porcellus | Etti, S | Gunasekaran, K | Karthe, P | Shanmugam, G | Heme | Hemoglobin | Iron | Metal-binding | Oxygen transport | Oxyhemoglobin | Transport
