6ofb: Difference between revisions
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==Crystal structure of human glutamine-dependent NAD+ synthetase complexed with NaAD+, AMP, pyrophosphate, and Mg2+== | |||
<StructureSection load='6ofb' size='340' side='right'caption='[[6ofb]], [[Resolution|resolution]] 2.84Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6ofb]] is a 2 chain structure. 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> | |||
</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> | |||
[[Category: | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6ofc|6ofc]]</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> | |||
== 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> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Chuenchor, W]] | |||
[[Category: Doukov, T I]] | |||
[[Category: Gerratana, B]] | [[Category: Gerratana, B]] | ||
[[Category: | [[Category: Ammonia tunneling]] | ||
[[Category: | [[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]] | |||
Revision as of 07:36, 8 January 2020
Crystal structure of human glutamine-dependent NAD+ synthetase complexed with NaAD+, AMP, pyrophosphate, and Mg2+
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