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3urh
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3urh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Sinorhizobium_meliloti Sinorhizobium meliloti]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3URH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3URH FirstGlance]. <br> | <table><tr><td colspan='2'>[[3urh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Sinorhizobium_meliloti Sinorhizobium meliloti]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3URH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3URH FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lpdA2, R03048, SMc02487 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=382 Sinorhizobium meliloti])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lpdA2, R03048, SMc02487 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=382 Sinorhizobium meliloti])</td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyl_dehydrogenase Dihydrolipoyl dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.4 1.8.1.4] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrolipoyl_dehydrogenase Dihydrolipoyl dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.4 1.8.1.4] </span></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=3urh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3urh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3urh RCSB], [http://www.ebi.ac.uk/pdbsum/3urh PDBsum]</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=3urh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3urh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3urh RCSB], [http://www.ebi.ac.uk/pdbsum/3urh PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
==See Also== | ==See Also== | ||
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[[Category: Dihydrolipoyl dehydrogenase]] | [[Category: Dihydrolipoyl dehydrogenase]] | ||
[[Category: Sinorhizobium meliloti]] | [[Category: Sinorhizobium meliloti]] | ||
| - | [[Category: Almo, S C | + | [[Category: Almo, S C]] |
| - | [[Category: Chamala, S | + | [[Category: Chamala, S]] |
| - | [[Category: Evans, B | + | [[Category: Evans, B]] |
| - | [[Category: Foti, R | + | [[Category: Foti, R]] |
| - | [[Category: Gizzi, A | + | [[Category: Gizzi, A]] |
| - | [[Category: Hillerich, B | + | [[Category: Hillerich, B]] |
| - | [[Category: Kar, A | + | [[Category: Kar, A]] |
| - | [[Category: Kumaran, D | + | [[Category: Kumaran, D]] |
| - | [[Category: LaFleur, J | + | [[Category: LaFleur, J]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | [[Category: Seidel, R | + | [[Category: Seidel, R]] |
| - | [[Category: Swaminathan, S | + | [[Category: Swaminathan, S]] |
| - | [[Category: Villigas, G | + | [[Category: Villigas, G]] |
| - | [[Category: Zencheck, W | + | [[Category: Zencheck, W]] |
[[Category: Dehydrogenase]] | [[Category: Dehydrogenase]] | ||
[[Category: Dihydrolipoamide]] | [[Category: Dihydrolipoamide]] | ||
[[Category: Dihydrolipoamide dehydrogenase]] | [[Category: Dihydrolipoamide dehydrogenase]] | ||
| - | [[Category: New york structural genomics research consortium]] | ||
[[Category: Nysgrc]] | [[Category: Nysgrc]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
| - | [[Category: Protein structure initiative]] | + | [[Category: PSI, Protein structure initiative]] |
[[Category: Psi-biology]] | [[Category: Psi-biology]] | ||
[[Category: Rossmann fold]] | [[Category: Rossmann fold]] | ||
| - | [[Category: Structural genomic]] | ||
Revision as of 10:55, 4 January 2015
Crystal structure of a dihydrolipoamide dehydrogenase from Sinorhizobium meliloti 1021
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Categories: Dihydrolipoyl dehydrogenase | Sinorhizobium meliloti | Almo, S C | Chamala, S | Evans, B | Foti, R | Gizzi, A | Hillerich, B | Kar, A | Kumaran, D | LaFleur, J | Structural genomic | Seidel, R | Swaminathan, S | Villigas, G | Zencheck, W | Dehydrogenase | Dihydrolipoamide | Dihydrolipoamide dehydrogenase | Nysgrc | Oxidoreductase | PSI, Protein structure initiative | Psi-biology | Rossmann fold
