4ga5: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| (2 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Crystal structure of AMP phosphorylase C-terminal deletion mutant in the apo-form== | ==Crystal structure of AMP phosphorylase C-terminal deletion mutant in the apo-form== | ||
<StructureSection load='4ga5' size='340' side='right' caption='[[4ga5]], [[Resolution|resolution]] 3.25Å' scene=''> | <StructureSection load='4ga5' size='340' side='right'caption='[[4ga5]], [[Resolution|resolution]] 3.25Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ga5]] is a 8 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4ga5]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_kodakarensis_KOD1 Thermococcus kodakarensis KOD1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GA5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GA5 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.25Å</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=4ga5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ga5 OCA], [https://pdbe.org/4ga5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ga5 RCSB], [https://www.ebi.ac.uk/pdbsum/4ga5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ga5 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/AMPPA_THEKO AMPPA_THEKO] Catalyzes the conversion of AMP and phosphate to adenine and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase activity toward CMP, dCMP and UMP in addition to AMP. Functions in an archaeal AMP degradation pathway, together with R15P isomerase and RubisCO.<ref>PMID:17303759</ref> <ref>PMID:23065974</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 16: | Line 17: | ||
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 4ga5" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Aono | [[Category: Thermococcus kodakarensis KOD1]] | ||
[[Category: Atomi | [[Category: Aono R]] | ||
[[Category: Imanaka | [[Category: Atomi H]] | ||
[[Category: Miki | [[Category: Imanaka T]] | ||
[[Category: Nakamura | [[Category: Miki K]] | ||
[[Category: Nishitani | [[Category: Nakamura A]] | ||
[[Category: Sato | [[Category: Nishitani Y]] | ||
[[Category: Sato T]] | |||