2vzl
From Proteopedia
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<StructureSection load='2vzl' size='340' side='right' caption='[[2vzl]], [[Resolution|resolution]] 1.93Å' scene=''> | <StructureSection load='2vzl' size='340' side='right' caption='[[2vzl]], [[Resolution|resolution]] 1.93Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2vzl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Nostoc_sp. Nostoc sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VZL OCA]. <br> | + | <table><tr><td colspan='2'>[[2vzl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Nostoc_sp. Nostoc sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VZL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VZL FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qgy|1qgy]], [[1h85|1h85]], [[1h42|1h42]], [[1qh0|1qh0]], [[2bmw|2bmw]], [[1go2|1go2]], [[1qgz|1qgz]], [[1ogj|1ogj]], [[1b2r|1b2r]], [[1ewy|1ewy]], [[1gjr|1gjr]], [[1que|1que]], [[1w87|1w87]], [[1w34|1w34]], [[1quf|1quf]], [[1e64|1e64]], [[2bsa|2bsa]], [[1gr1|1gr1]], [[1ogi|1ogi]], [[1w35|1w35]], [[1bjk|1bjk]], [[1e63|1e63]], [[1bqe|1bqe]], [[1e62|1e62]], [[2vyq|2vyq]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qgy|1qgy]], [[1h85|1h85]], [[1h42|1h42]], [[1qh0|1qh0]], [[2bmw|2bmw]], [[1go2|1go2]], [[1qgz|1qgz]], [[1ogj|1ogj]], [[1b2r|1b2r]], [[1ewy|1ewy]], [[1gjr|1gjr]], [[1que|1que]], [[1w87|1w87]], [[1w34|1w34]], [[1quf|1quf]], [[1e64|1e64]], [[2bsa|2bsa]], [[1gr1|1gr1]], [[1ogi|1ogi]], [[1w35|1w35]], [[1bjk|1bjk]], [[1e63|1e63]], [[1bqe|1bqe]], [[1e62|1e62]], [[2vyq|2vyq]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ferredoxin--NADP(+)_reductase Ferredoxin--NADP(+) reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.1.2 1.18.1.2] </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=2vzl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vzl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vzl RCSB], [http://www.ebi.ac.uk/pdbsum/2vzl 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=2vzl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vzl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vzl RCSB], [http://www.ebi.ac.uk/pdbsum/2vzl PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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Protein motifs involved in coenzyme interaction and enzymatic efficiency in anabaena ferredoxin-NADP+ reductase.,Peregrina JR, Herguedas B, Hermoso JA, Martinez-Julvez M, Medina M Biochemistry. 2009 Apr 14;48(14):3109-19. PMID:19219975<ref>PMID:19219975</ref> | Protein motifs involved in coenzyme interaction and enzymatic efficiency in anabaena ferredoxin-NADP+ reductase.,Peregrina JR, Herguedas B, Hermoso JA, Martinez-Julvez M, Medina M Biochemistry. 2009 Apr 14;48(14):3109-19. PMID:19219975<ref>PMID:19219975</ref> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
== References == | == References == | ||
Revision as of 06:08, 10 October 2014
FERREDOXIN-NADP REDUCTASE (MUTATIONS: T155G, A160T, L263P AND Y303S) COMPLEXED WITH NAD BY COCRYSTALLIZATION
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