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4rzh
From Proteopedia
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==Crystal structure of FabG from Synechocystis sp. PCC 6803== | ==Crystal structure of FabG from Synechocystis sp. PCC 6803== | ||
| - | <StructureSection load='4rzh' size='340' side='right' caption='[[4rzh]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='4rzh' size='340' side='right'caption='[[4rzh]], [[Resolution|resolution]] 2.20Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4rzh]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RZH OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[4rzh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803 Synechocystis sp. PCC 6803]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RZH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RZH 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]] 2.2Å</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=4rzh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rzh OCA], [https://pdbe.org/4rzh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rzh RCSB], [https://www.ebi.ac.uk/pdbsum/4rzh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rzh ProSAT]</span></td></tr> |
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FABG_SYNY3 FABG_SYNY3] Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis (Probable). Is capable of reducing acetoacetyl-CoA, but less well than its paralog PhaB (PubMed:26358291).<ref>PMID:26358291</ref> <ref>PMID:26358291</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Synechocystis sp. PCC 6803]] |
| - | [[Category: | + | [[Category: Liu Y]] |
| - | [[Category: | + | [[Category: Xue S]] |
Current revision
Crystal structure of FabG from Synechocystis sp. PCC 6803
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