2vig
From Proteopedia
(Difference between revisions)
Line 3: | Line 3: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2vig]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VIG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VIG FirstGlance]. <br> | <table><tr><td colspan='2'>[[2vig]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VIG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VIG FirstGlance]. <br> | ||
- | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COS:COENZYME+A+PERSULFIDE'>COS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COS:COENZYME+A+PERSULFIDE'>COS</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> |
- | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Butyryl-CoA_dehydrogenase Butyryl-CoA dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.2 1.3.99.2] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Butyryl-CoA_dehydrogenase Butyryl-CoA dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.2 1.3.99.2] </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=2vig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vig OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vig RCSB], [http://www.ebi.ac.uk/pdbsum/2vig 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=2vig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vig OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vig RCSB], [http://www.ebi.ac.uk/pdbsum/2vig PDBsum]</span></td></tr> |
- | <table> | + | </table> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Line 24: | Line 24: | ||
[[Category: Butyryl-CoA dehydrogenase]] | [[Category: Butyryl-CoA dehydrogenase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
- | [[Category: Arrowsmith, C H | + | [[Category: Arrowsmith, C H]] |
- | [[Category: Delft, F Von | + | [[Category: Delft, F Von]] |
- | [[Category: Edwards, A | + | [[Category: Edwards, A]] |
- | [[Category: Gileadi, O | + | [[Category: Gileadi, O]] |
- | [[Category: Oppermann, U | + | [[Category: Oppermann, U]] |
- | [[Category: Pantic, N | + | [[Category: Pantic, N]] |
- | [[Category: Parizotto, E | + | [[Category: Parizotto, E]] |
- | [[Category: Pike, A C.W | + | [[Category: Pike, A C.W]] |
- | [[Category: Ugochukwu, E | + | [[Category: Ugochukwu, E]] |
- | [[Category: Weigelt, J | + | [[Category: Weigelt, J]] |
[[Category: Beta oxidation]] | [[Category: Beta oxidation]] | ||
[[Category: Disease mutation]] | [[Category: Disease mutation]] |
Revision as of 13:11, 19 January 2015
CRYSTAL STRUCTURE OF HUMAN SHORT-CHAIN ACYL COA DEHYDROGENASE
|
Categories: Butyryl-CoA dehydrogenase | Homo sapiens | Arrowsmith, C H | Delft, F Von | Edwards, A | Gileadi, O | Oppermann, U | Pantic, N | Parizotto, E | Pike, A C.W | Ugochukwu, E | Weigelt, J | Beta oxidation | Disease mutation | Fad | Fatty acid metabolism | Flavoprotein | Lipid metabolism | Mitochondrion | Oxidoreductase | Transit peptide