6ofb: Difference between revisions

No edit summary
No edit summary
 
(One intermediate revision by the same user not shown)
Line 3: Line 3:
<StructureSection load='6ofb' size='340' side='right'caption='[[6ofb]], [[Resolution|resolution]] 2.84&Aring;' scene=''>
<StructureSection load='6ofb' size='340' side='right'caption='[[6ofb]], [[Resolution|resolution]] 2.84&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6ofb]] 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=6OFB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OFB FirstGlance]. <br>
<table><tr><td colspan='2'>[[6ofb]] 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=6OFB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OFB FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DND:NICOTINIC+ACID+ADENINE+DINUCLEOTIDE'>DND</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</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]] 2.84&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6ofc|6ofc]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DND:NICOTINIC+ACID+ADENINE+DINUCLEOTIDE'>DND</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NADSYN1 ([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=6ofb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ofb OCA], [https://pdbe.org/6ofb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ofb RCSB], [https://www.ebi.ac.uk/pdbsum/6ofb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ofb ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(+)_synthase_(glutamine-hydrolyzing) NAD(+) synthase (glutamine-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.5.1 6.3.5.1] </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=6ofb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ofb OCA], [http://pdbe.org/6ofb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ofb RCSB], [http://www.ebi.ac.uk/pdbsum/6ofb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ofb ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/NADE_HUMAN NADE_HUMAN]] Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD (PubMed:12547821). Uses L-glutamine as a nitrogen source (PubMed:12547821).<ref>PMID:12547821</ref>
[https://www.uniprot.org/uniprot/NADE_HUMAN NADE_HUMAN] Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD (PubMed:12547821). Uses L-glutamine as a nitrogen source (PubMed:12547821).<ref>PMID:12547821</ref>  
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 21: Line 19:
</div>
</div>
<div class="pdbe-citations 6ofb" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6ofb" style="background-color:#fffaf0;"></div>
==See Also==
*[[NAD synthase|NAD synthase]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Chuenchor, W]]
[[Category: Chuenchor W]]
[[Category: Doukov, T I]]
[[Category: Doukov TI]]
[[Category: Gerratana, B]]
[[Category: Gerratana B]]
[[Category: Ammonia tunneling]]
[[Category: Atp-binding]]
[[Category: Enzyme]]
[[Category: Gat]]
[[Category: Glutaminase]]
[[Category: Glutamine-amido transferase]]
[[Category: Glutamine-dependent nad+ synthetase]]
[[Category: Ligase]]
[[Category: Nad synthetase 1]]
[[Category: Nad+ synthetase]]
[[Category: Nucleotide-binding]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA