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5a8k
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==METHYL-COENZYME M REDUCTASE FROM METHANOTHERMOBACTER WOLFEII AT 1.4 A RESOLUTION== | |
| - | + | <StructureSection load='5a8k' size='340' side='right' caption='[[5a8k]], [[Resolution|resolution]] 1.41Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5a8k]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_wolfeii Methanothermobacter wolfeii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A8K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A8K FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=COM:1-THIOETHANESULFONIC+ACID'>COM</scene>, <scene name='pdbligand=ETX:2-ETHOXYETHANOL'>ETX</scene>, <scene name='pdbligand=F43:FACTOR+430'>F43</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TP7:COENZYME+B'>TP7</scene></td></tr> | |
| - | [[Category: | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=AGM:5-METHYL-ARGININE'>AGM</scene>, <scene name='pdbligand=GL3:THIOGLYCIN'>GL3</scene>, <scene name='pdbligand=MGN:2-METHYL-GLUTAMINE'>MGN</scene>, <scene name='pdbligand=MHS:N1-METHYLATED+HISTIDINE'>MHS</scene>, <scene name='pdbligand=SMC:S-METHYLCYSTEINE'>SMC</scene></td></tr> |
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5a8r|5a8r]], [[5a8w|5a8w]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Coenzyme-B_sulfoethylthiotransferase Coenzyme-B sulfoethylthiotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.8.4.1 2.8.4.1] </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=5a8k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a8k OCA], [http://pdbe.org/5a8k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a8k RCSB], [http://www.ebi.ac.uk/pdbsum/5a8k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5a8k ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Coenzyme-B sulfoethylthiotransferase]] | ||
| + | [[Category: Methanothermobacter wolfeii]] | ||
| + | [[Category: Ermler, U]] | ||
[[Category: Wagner, T]] | [[Category: Wagner, T]] | ||
| - | [[Category: | + | [[Category: Binding site]] |
| + | [[Category: Catalysis]] | ||
| + | [[Category: Coenzyme]] | ||
| + | [[Category: Disulfide]] | ||
| + | [[Category: Hydrogen]] | ||
| + | [[Category: Hydrogen bonding]] | ||
| + | [[Category: Ligand]] | ||
| + | [[Category: Mesna]] | ||
| + | [[Category: Metalloporphyrin]] | ||
| + | [[Category: Methane]] | ||
| + | [[Category: Methanobacterium]] | ||
| + | [[Category: Model]] | ||
| + | [[Category: Molecular]] | ||
| + | [[Category: Nickel]] | ||
| + | [[Category: Oxidation-reduction]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Phosphothreonine]] | ||
| + | [[Category: Post-translational modification]] | ||
| + | [[Category: Protein conformation]] | ||
| + | [[Category: Protein folding]] | ||
| + | [[Category: Protein structure]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 04:09, 4 August 2016
METHYL-COENZYME M REDUCTASE FROM METHANOTHERMOBACTER WOLFEII AT 1.4 A RESOLUTION
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Categories: Coenzyme-B sulfoethylthiotransferase | Methanothermobacter wolfeii | Ermler, U | Wagner, T | Binding site | Catalysis | Coenzyme | Disulfide | Hydrogen | Hydrogen bonding | Ligand | Mesna | Metalloporphyrin | Methane | Methanobacterium | Model | Molecular | Nickel | Oxidation-reduction | Oxidoreductase | Phosphothreonine | Post-translational modification | Protein conformation | Protein folding | Protein structure | Transferase
