1a7d: Difference between revisions

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 ==CHLOROMET MYOHEMERYTHRIN FROM THEMISTE ZOSTERICOLA==
-<StructureSection load='1a7d' size='340' side='right' caption='[[1a7d]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+<StructureSection load='1a7d' size='340' side='right'caption='[[1a7d]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1a7d]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Themiste_hennahi Themiste hennahi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A7D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1A7D FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1a7d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Themiste_hennahi Themiste hennahi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A7D FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CFO:CHLORO+DIIRON-OXO+MOIETY'>CFO</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene><br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</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=1a7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a7d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1a7d RCSB], [http://www.ebi.ac.uk/pdbsum/1a7d PDBsum]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CFO:CHLORO+DIIRON-OXO+MOIETY'>CFO</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
-<table>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a7d OCA], [https://pdbe.org/1a7d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a7d RCSB], [https://www.ebi.ac.uk/pdbsum/1a7d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a7d ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/HEMTM_THEHE HEMTM_THEHE] Myohemerythrin is an oxygen-binding protein found in the retractor muscles of certain worms. The oxygen-binding site contains two iron atoms.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
    <jmolCheckbox>
-     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a7/1a7d_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a7/1a7d_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
    </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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=1a7d ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Myohemerythrin (Mhr) is a nonheme iron oxygen carrier found in the retractor muscles of marine "peanut" worms. The X-ray crystal structures of two recombinant Themiste zostericola Mhrs are reported to a resolution of 1.8 A. Surprisingly, the met wild-type structure (R = 17.8%) was found to contain chloride bound to Fe2, while coordinated hydroxide was found in the met L103N structure (R = 18.3%). An internal water molecule was also found distal to the Fe-O-Fe center of the mutant protein, forming hydrogen bonds with the coordinated hydroxide and the OD1 atom of Asn-103. This finding is consistent with the kinetic and spectroscopic results reported for the L103N mutant Mhr [Raner, G. M., Martins, L. J., &amp; Ellis, W. R., Jr. (1997) Biochemistry 36, 7037-7043]. Possible roles for the side chain of residue 103 (Leu in wild-type Mhr) in gating ligand binding are also discussed.
-Structures of wild-type chloromet and L103N hydroxomet Themiste zostericola myohemerythrins at 1.8 A resolution.,Martins LJ, Hill CP, Ellis WR Jr Biochemistry. 1997 Jun 10;36(23):7044-9. PMID:9188702<ref>PMID:9188702</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Themiste hennahi]]
-[[Category: Hill, C P.]]
+[[Category: Ellis Junior WR]]
-[[Category: Junior, W R.Ellis.]]
+[[Category: Hill CP]]
-[[Category: Martins, L J.]]
+[[Category: Martins LJ]]
-[[Category: Nonheme iron oxygen carrier]]
-[[Category: Oxygen transport]]