2eb9: Difference between revisions
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<StructureSection load='2eb9' size='340' side='right'caption='[[2eb9]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='2eb9' size='340' side='right'caption='[[2eb9]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2eb9]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2eb9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Phycd Phycd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EB9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EB9 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CUS:(N-SALICYLIDEN-L-LEUCINATO)-COPPER(II)'>CUS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CUS:(N-SALICYLIDEN-L-LEUCINATO)-COPPER(II)'>CUS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2eb8|2eb8]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2eb8|2eb8]]</div></td></tr> | ||
<tr id='resources'><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=2eb9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eb9 OCA], [https://pdbe.org/2eb9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2eb9 RCSB], [https://www.ebi.ac.uk/pdbsum/2eb9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2eb9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC]] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] |
Revision as of 20:22, 15 December 2021
Crystal Structure of Cu(II)(Sal-Leu)/apo-MyoglobinCrystal Structure of Cu(II)(Sal-Leu)/apo-Myoglobin
Structural highlights
Function[MYG_PHYMC] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedapo-Myoglobin (apo-Mb) was reconstituted with three copper complexes: CuII(Sal-Phe) (1; Sal-Phe = N-salicylidene-L-phenylalanato), CuII(Sal-Leu) (2; Sal-Leu = N-salicylidene-L-leucinato), and CuII(Sal-Ala) (3; Sal-Ala = N-salicylidene-L-alanato). The crystal structures of 1.apo-Mb (1.65 Angstrom resolution) and 2.apo-Mb (1.8 Angstrom resolution) show that the coordination geometry around the CuII atom in apo-Mb is distorted square-planar with tridentate Sal-X and a Nepsilon atom of His64 in the apo-Mb cavity and the plane of these copper complexes is perpendicular to that of heme. These results suggest that the apo-Mb cavity can hold metal complexes with various coordination geometries. Design and structure analysis of artificial metalloproteins: selective coordination of His64 to copper complexes with square-planar structure in the apo-myoglobin scaffold.,Abe S, Ueno T, Reddy PA, Okazaki S, Hikage T, Suzuki A, Yamane T, Nakajima H, Watanabe Y Inorg Chem. 2007 Jun 25;46(13):5137-9. Epub 2007 May 25. PMID:17523632[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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