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3ej8
From Proteopedia
(Difference between revisions)
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==Structure of double mutant of human iNOS oxygenase domain with bound immidazole== | ==Structure of double mutant of human iNOS oxygenase domain with bound immidazole== | ||
<StructureSection load='3ej8' size='340' side='right' caption='[[3ej8]], [[Resolution|resolution]] 2.55Å' scene=''> | <StructureSection load='3ej8' size='340' side='right' caption='[[3ej8]], [[Resolution|resolution]] 2.55Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3ej8]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3ej8]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EJ8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EJ8 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=H4B:5,6,7,8-TETRAHYDROBIOPTERIN'>H4B</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=H4B:5,6,7,8-TETRAHYDROBIOPTERIN'>H4B</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3e65|3e65]], [[3e67|3e67]], [[3e68|3e68]], [[3e6l|3e6l]], [[3e6n|3e6n]], [[3e6o|3e6o]], [[3e6t|3e6t]], [[3e7g|3e7g]], [[3e7i|3e7i]], [[3e7m|3e7m]], [[3e7s|3e7s]], [[3e7t|3e7t]], [[3eah|3eah]], [[3eai|3eai]], [[3ebd|3ebd]], [[3ebf|3ebf]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3e65|3e65]], [[3e67|3e67]], [[3e68|3e68]], [[3e6l|3e6l]], [[3e6n|3e6n]], [[3e6o|3e6o]], [[3e6t|3e6t]], [[3e7g|3e7g]], [[3e7i|3e7i]], [[3e7m|3e7m]], [[3e7s|3e7s]], [[3e7t|3e7t]], [[3eah|3eah]], [[3eai|3eai]], [[3ebd|3ebd]], [[3ebf|3ebf]]</td></tr> | ||
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Nos2A, NOS2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Nos2A, NOS2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitric- | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nitric-oxide_synthase_(NADPH_dependent) Nitric-oxide synthase (NADPH dependent)], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ej8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ej8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ej8 RCSB], [http://www.ebi.ac.uk/pdbsum/3ej8 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=3ej8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ej8 OCA], [http://pdbe.org/3ej8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ej8 RCSB], [http://www.ebi.ac.uk/pdbsum/3ej8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ej8 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[http://www.uniprot.org/uniprot/ | + | [[http://www.uniprot.org/uniprot/NOS2_HUMAN NOS2_HUMAN]] 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. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| - | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3ej8 ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 3ej8" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Human]] |
| - | + | ||
[[Category: Aberg, A]] | [[Category: Aberg, A]] | ||
[[Category: Andersson, G]] | [[Category: Andersson, G]] | ||
Revision as of 04:22, 5 August 2016
Structure of double mutant of human iNOS oxygenase domain with bound immidazole
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Categories: Human | Aberg, A | Andersson, G | Andrews, G | Arvai, A S | Cheshire, D R | Connolly, S | Crane, B R | Garcin, E D | Gensmantel, N P | Getzoff, E D | Hamley, P J | Kroeger, M D | Mallinder, P R | Mete, A | Nicholls, D J | Rosenfeld, R J | St-Gallay, S A | Stuehr, D J | Tainer, J A | Tinker, A C | Wallace, A V | Fad | Fmn | Heme | Iron | Metal-binding | Nadp | Nitric oxide synthase | No | Oxidoreductase | Oxidoreductase calmodulin-binding | Tetrahydrobiopterin
