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1xsc
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1xsc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XSC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XSC FirstGlance]. <br> | <table><tr><td colspan='2'>[[1xsc]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XSC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XSC FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1xsa|1xsa]], [[1xsb|1xsb]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1xsa|1xsa]], [[1xsb|1xsb]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Bis(5'-nucleosyl)-tetraphosphatase_(asymmetrical) Bis(5'-nucleosyl)-tetraphosphatase (asymmetrical)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.17 3.6.1.17] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Bis(5'-nucleosyl)-tetraphosphatase_(asymmetrical) Bis(5'-nucleosyl)-tetraphosphatase (asymmetrical)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.17 3.6.1.17] </span></td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xsc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xsc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1xsc RCSB], [http://www.ebi.ac.uk/pdbsum/1xsc PDBsum]</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=1xsc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xsc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1xsc RCSB], [http://www.ebi.ac.uk/pdbsum/1xsc PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/AP4A_HUMAN AP4A_HUMAN]] Asymmetrically hydrolyzes Ap4A to yield AMP and ATP. Plays a major role in maintaining homeostasis. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Buyya, S | + | [[Category: Buyya, S]] |
| - | [[Category: Gayler, K R | + | [[Category: Gayler, K R]] |
| - | [[Category: Gooley, P R | + | [[Category: Gooley, P R]] |
| - | [[Category: Gunawardana, D | + | [[Category: Gunawardana, D]] |
| - | [[Category: McLennan, A G | + | [[Category: McLennan, A G]] |
| - | [[Category: Swarbrick, J D | + | [[Category: Swarbrick, J D]] |
[[Category: Alpha-beta]] | [[Category: Alpha-beta]] | ||
[[Category: Human ap4a atp hydrolase]] | [[Category: Human ap4a atp hydrolase]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Nudix enzyme]] | [[Category: Nudix enzyme]] | ||
Revision as of 08:09, 24 December 2014
Structure of the nudix enzyme AP4A hydrolase from homo sapiens (E63A mutant) in complex with ATP
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