5c6e

<StructureSection load='5c6e' size='340' side='right' caption='[[5c6e]], [[Resolution|resolution]] 1.70&Aring;' scene=''>

<table><tr><td colspan='2'>[[5c6e]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C6E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C6E FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5c8i|5c8i]], [[5ccd|5ccd]]</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=5c6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c6e OCA], [http://pdbe.org/5c6e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c6e RCSB], [http://www.ebi.ac.uk/pdbsum/5c6e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5c6e ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/HBA_HORSE HBA_HORSE]] Involved in oxygen transport from the lung to the various peripheral tissues. [[http://www.uniprot.org/uniprot/HBB_HORSE HBB_HORSE]] Involved in oxygen transport from the lung to the various peripheral tissues.

X-ray and neutron crystallographic techniques provide complementary information on the structure and function of biological macromolecules. X-ray and neutron (XN) crystallographic data have been combined in a joint structure-refinement procedure that has been developed using recent advances in modern computational methodologies, including cross-validated maximum-likelihood target functions with gradient-based optimization and simulated annealing. The XN approach for complete (including hydrogen) macromolecular structure analysis provides more accurate and complete structures, as demonstrated for diisopropyl fluorophosphatase, photoactive yellow protein and human aldose reductase. Furthermore, this method has several practical advantages, including the easier determination of the orientation of water molecules, hydroxyl groups and some amino-acid side chains.

 

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== References ==

[[Category: Dajnowicz, S]]

[[Category: Fisher, S Z]]

[[Category: Hanson, B L]]

[[Category: Kovalevsky, A Y]]

[[Category: Langan, P]]

[[Category: Mueser, T C]]

[[Category: Sean, S]]

[[Category: R-state]]