2e5w: Difference between revisions
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<StructureSection load='2e5w' size='340' side='right'caption='[[2e5w]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='2e5w' size='340' side='right'caption='[[2e5w]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2e5w]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2e5w]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E5W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E5W FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=AG3:1-{4-[(3-AMINOPROPYL)AMINO]BUTYL}GUANIDINE'>AG3</scene>, <scene name='pdbligand=MTA:5-DEOXY-5-METHYLTHIOADENOSINE'>MTA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=AG3:1-{4-[(3-AMINOPROPYL)AMINO]BUTYL}GUANIDINE'>AG3</scene>, <scene name='pdbligand=MTA:5-DEOXY-5-METHYLTHIOADENOSINE'>MTA</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Spermidine_synthase Spermidine synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.16 2.5.1.16] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2e5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e5w OCA], [https://pdbe.org/2e5w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e5w RCSB], [https://www.ebi.ac.uk/pdbsum/2e5w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e5w ProSAT], [https://www.topsan.org/Proteins/RSGI/2e5w TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/SPEE_PYRHO SPEE_PYRHO]] Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine (By similarity).[HAMAP-Rule:MF_00198] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 10:33, 2 February 2022
Crystal structure of spermidine synthase from Pyrococcus horikoshii OT3Crystal structure of spermidine synthase from Pyrococcus horikoshii OT3
Structural highlights
Function[SPEE_PYRHO] Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine (By similarity).[HAMAP-Rule:MF_00198] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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