1s98: Difference between revisions
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<StructureSection load='1s98' size='340' side='right'caption='[[1s98]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='1s98' size='340' side='right'caption='[[1s98]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1s98]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1s98]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S98 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S98 FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YFHF, B2528, C3053, Z3795, ECS3394, SF2575, S2747 ([ | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YFHF, B2528, C3053, Z3795, ECS3394, SF2575, S2747 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=1s98 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s98 OCA], [https://pdbe.org/1s98 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s98 RCSB], [https://www.ebi.ac.uk/pdbsum/1s98 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s98 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/ISCA_ECOLI ISCA_ECOLI]] Is able to transfer iron-sulfur clusters to apo-ferredoxin. Multiple cycles of [2Fe2S] cluster formation and transfer are observed, suggesting that IscA acts catalytically. Recruits intracellular free iron so as to provide iron for the assembly of transient iron-sulfur cluster in IscU in the presence of IscS, L-cysteine and the thioredoxin reductase system TrxA/TrxB.[HAMAP-Rule:MF_01429] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||