1mmo: Difference between revisions

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 <StructureSection load='1mmo' size='340' side='right'caption='[[1mmo]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1mmo]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Acm_1292 Acm 1292]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MMO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MMO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1mmo]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylococcus_capsulatus Methylococcus capsulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MMO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MMO FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methane_monooxygenase_(soluble) Methane monooxygenase (soluble)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.25 1.14.13.25] </span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></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=1mmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mmo OCA], [http://pdbe.org/1mmo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mmo RCSB], [http://www.ebi.ac.uk/pdbsum/1mmo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mmo ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mmo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mmo OCA], [https://pdbe.org/1mmo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mmo RCSB], [https://www.ebi.ac.uk/pdbsum/1mmo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mmo ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MEMB_METCA MEMB_METCA]] Responsible for the initial oxygenation of methane to methanol in methanotrophs. It also catalyzes the monohydroxylation of a variety of unactivated alkenes, alicyclic, aromatic and heterocyclic compounds. [[http://www.uniprot.org/uniprot/MEMG_METCA MEMG_METCA]] Responsible for the initial oxygenation of methane to methanol in methanotrophs. It also catalyzes the monohydroxylation of a variety of unactivated alkenes, alicyclic, aromatic and heterocyclic compounds. [[http://www.uniprot.org/uniprot/MEMA_METCA MEMA_METCA]] Responsible for the initial oxygenation of methane to methanol in methanotrophs. It also catalyzes the monohydroxylation of a variety of unactivated alkenes, alicyclic, aromatic and heterocyclic compounds.
+[https://www.uniprot.org/uniprot/MEMA_METCA MEMA_METCA] Responsible for the initial oxygenation of methane to methanol in methanotrophs. It also catalyzes the monohydroxylation of a variety of unactivated alkenes, alicyclic, aromatic and heterocyclic compounds.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </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=1mmo ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The 2.2 A crystal structure of the 251K alpha 2 beta 2 gamma 2 dimeric hydroxylase protein of methane monooxygenase from Methylococcus capsulatus (Bath) reveals the geometry of the catalytic di-iron core. The two iron atoms are bridged by exogenous hydroxide and acetate ligands and further coordinated by four glutamate residues, two histidine residues and a water molecule. The dinuclear iron centre lies in a hydrophobic active-site cavity for binding methane. An extended canyon runs between alpha beta pairs, which have many long alpha-helices, for possible docking of the reductase and coupling proteins required for catalysis.
-Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane.,Rosenzweig AC, Frederick CA, Lippard SJ, Nordlund P Nature. 1993 Dec 9;366(6455):537-43. PMID:8255292<ref>PMID:8255292</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1mmo" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Methane monooxygenase|Methane monooxygenase]]
+*[[Methane monooxygenase 3D structures|Methane monooxygenase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Acm 1292]]
 [[Category: Large Structures]]
-[[Category: Frederick, C A]]
+[[Category: Methylococcus capsulatus]]
-[[Category: Lippard, S J]]
+[[Category: Frederick CA]]
-[[Category: Nordlund, P]]
+[[Category: Lippard SJ]]
-[[Category: Rosenzweig, A C]]
+[[Category: Nordlund P]]
+[[Category: Rosenzweig AC]]