1nut: Difference between revisions

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<StructureSection load='1nut' size='340' side='right'caption='[[1nut]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='1nut' size='340' side='right'caption='[[1nut]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1nut]] is a 2 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=1NUT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1NUT FirstGlance]. <br>
<table><tr><td colspan='2'>[[1nut]] is a 2 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=1NUT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NUT FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.9&#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;'>[[1nup|1nup]], [[1nuq|1nuq]], [[1nur|1nur]], [[1nus|1nus]], [[1nuu|1nuu]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FKSG76 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=1nut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nut OCA], [https://pdbe.org/1nut PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nut RCSB], [https://www.ebi.ac.uk/pdbsum/1nut PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nut ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1nut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nut OCA], [http://pdbe.org/1nut PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nut RCSB], [http://www.ebi.ac.uk/pdbsum/1nut PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1nut ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/NMNA3_HUMAN NMNA3_HUMAN]] Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency. Can use triazofurin monophosphate (TrMP) as substrate. Can also use GTP and ITP as nucleotide donors. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity, can use NAD (+), NADH, NAAD, nicotinic acid adenine dinucleotide phosphate (NHD), nicotinamide guanine dinucleotide (NGD) as substrates. Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NAADP(+). Protects against axonal degeneration following injury.<ref>PMID:16118205</ref> <ref>PMID:17402747</ref>
[https://www.uniprot.org/uniprot/NMNA3_HUMAN NMNA3_HUMAN] Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency. Can use triazofurin monophosphate (TrMP) as substrate. Can also use GTP and ITP as nucleotide donors. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity, can use NAD (+), NADH, NAAD, nicotinic acid adenine dinucleotide phosphate (NHD), nicotinamide guanine dinucleotide (NGD) as substrates. Fails to cleave phosphorylated dinucleotides NADP(+), NADPH and NAADP(+). Protects against axonal degeneration following injury.<ref>PMID:16118205</ref> <ref>PMID:17402747</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Grishin, N V]]
[[Category: Grishin NV]]
[[Category: Karthikeyan, S]]
[[Category: Karthikeyan S]]
[[Category: Kurnasov, O V]]
[[Category: Kurnasov OV]]
[[Category: Osterman, A L]]
[[Category: Osterman AL]]
[[Category: Zhang, H]]
[[Category: Zhang H]]
[[Category: Zhang, X]]
[[Category: Zhang X]]
[[Category: Enzyme catalysis]]
[[Category: Mitochondria]]
[[Category: Nad biosynthesis]]
[[Category: Pyridine adenylyltransferase]]
[[Category: Transferase]]
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