2wmd: Difference between revisions

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<StructureSection load='2wmd' size='340' side='right'caption='[[2wmd]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='2wmd' size='340' side='right'caption='[[2wmd]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2wmd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WMD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WMD FirstGlance]. <br>
<table><tr><td colspan='2'>[[2wmd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WMD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WMD FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=ZZ0:2-(4-CHLORO-PHENYLAMINO)-NICOTINIC+ACID'>ZZ0</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2wm3|2wm3]], [[2exx|2exx]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=ZZ0:2-(4-CHLORO-PHENYLAMINO)-NICOTINIC+ACID'>ZZ0</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2wmd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wmd OCA], [https://pdbe.org/2wmd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wmd RCSB], [https://www.ebi.ac.uk/pdbsum/2wmd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wmd ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2wmd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wmd OCA], [https://pdbe.org/2wmd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wmd RCSB], [https://www.ebi.ac.uk/pdbsum/2wmd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wmd ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NMRL1_HUMAN NMRL1_HUMAN] Redox sensor protein. Undergoes restructuring and subcellular redistribution in response to changes in intracellular NADPH/NADP(+) levels. At low NADPH concentrations the protein is found mainly as a monomer, and binds argininosuccinate synthase (ASS1), the enzyme involved in nitric oxide synthesis. Association with ASS1 impairs its activity and reduces the production of nitric oxide, which subsecuently prevents apoptosis. Under normal NADPH concentrations, the protein is found as a dimer and hides the binding site for ASS1. The homodimer binds one molecule of NADPH. Has higher affinity for NADPH than for NADP(+). Binding to NADPH is necessary to form a stable dimer.<ref>PMID:18263583</ref> <ref>PMID:17496144</ref> <ref>PMID:19254724</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=2wmd ConSurf].
</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=2wmd ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C]]
[[Category: Arrowsmith C]]
[[Category: Bhatia, C]]
[[Category: Bhatia C]]
[[Category: Bountra, C]]
[[Category: Bountra C]]
[[Category: Delft, F von]]
[[Category: Edwards A]]
[[Category: Edwards, A]]
[[Category: Filippakopoulos P]]
[[Category: Filippakopoulos, P]]
[[Category: Heightman T]]
[[Category: Heightman, T]]
[[Category: Hozjan V]]
[[Category: Hozjan, V]]
[[Category: Niesen F]]
[[Category: Niesen, F]]
[[Category: Oppermann U]]
[[Category: Oppermann, U]]
[[Category: Pilka E]]
[[Category: Pilka, E]]
[[Category: Roos AK]]
[[Category: Roos, A K]]
[[Category: Savitsky P]]
[[Category: Savitsky, P]]
[[Category: Ugochukwu E]]
[[Category: Ugochukwu, E]]
[[Category: Weigelt J]]
[[Category: Weigelt, J]]
[[Category: Yue WW]]
[[Category: Yue, W W]]
[[Category: Von Delft F]]
[[Category: Disulfide bond]]
[[Category: Oxidoreductase]]

Latest revision as of 10:14, 9 May 2024

Crystal structure of NmrA-like family domain containing protein 1 in complex with NADP and 2-(4-chloro-phenylamino)-nicotinic acid

2wmd, resolution 2.00Å

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