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2bhj
From Proteopedia
(Difference between revisions)
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<StructureSection load='2bhj' size='340' side='right'caption='[[2bhj]], [[Resolution|resolution]] 3.20Å' scene=''> | <StructureSection load='2bhj' size='340' side='right'caption='[[2bhj]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2bhj]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2bhj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BHJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BHJ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FC1:THIOCOUMARIN'>FC1</scene>, <scene name='pdbligand=HBI:7,8-DIHYDROBIOPTERIN'>HBI</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FC1:THIOCOUMARIN'>FC1</scene>, <scene name='pdbligand=HBI:7,8-DIHYDROBIOPTERIN'>HBI</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dd7|1dd7]], [[1df1|1df1]], [[1dwv|1dwv]], [[1dww|1dww]], [[1dwx|1dwx]], [[1jwj|1jwj]], [[1jwk|1jwk]], [[1m8d|1m8d]], [[1m8e|1m8e]], [[1m8h|1m8h]], [[1m8i|1m8i]], [[1m9t|1m9t]], [[1n2n|1n2n]], [[1noc|1noc]], [[1nod|1nod]], [[1nos|1nos]], [[1qom|1qom]], [[1qw4|1qw4]], [[1qw5|1qw5]], [[1r35|1r35]], [[1vaf|1vaf]], [[2nod|2nod]], [[2nos|2nos]], [[3nod|3nod]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dd7|1dd7]], [[1df1|1df1]], [[1dwv|1dwv]], [[1dww|1dww]], [[1dwx|1dwx]], [[1jwj|1jwj]], [[1jwk|1jwk]], [[1m8d|1m8d]], [[1m8e|1m8e]], [[1m8h|1m8h]], [[1m8i|1m8i]], [[1m9t|1m9t]], [[1n2n|1n2n]], [[1noc|1noc]], [[1nod|1nod]], [[1nos|1nos]], [[1qom|1qom]], [[1qw4|1qw4]], [[1qw5|1qw5]], [[1r35|1r35]], [[1vaf|1vaf]], [[2nod|2nod]], [[2nos|2nos]], [[3nod|3nod]]</div></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Nitric-oxide_synthase_(NADPH_dependent) Nitric-oxide synthase (NADPH dependent)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.39 1.14.13.39] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bhj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bhj OCA], [https://pdbe.org/2bhj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bhj RCSB], [https://www.ebi.ac.uk/pdbsum/2bhj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bhj ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/NOS2_MOUSE NOS2_MOUSE]] Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such COX2.<ref>PMID:16373578</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 13:10, 24 November 2021
murine iNO synthase with coumarin inhibitor
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Categories: Large Structures | Lk3 transgenic mice | Guilloteau, J P | Mathieu, M | Calmodulin-binding | Fad | Fmn | Heme | Ino | Metal-binding | Nadp | Oxidoreductase | Polymorphism | Zinc

