6e97
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==Implication of MbtH-like proteins in crystallization of the independent NRPS A domains. Crystal structure of FscC: supporting rationale for revised mechanism of freestanding aryl acid adenylating enzymes.== | |
- | + | <StructureSection load='6e97' size='340' side='right'caption='[[6e97]], [[Resolution|resolution]] 1.80Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[6e97]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E97 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E97 FirstGlance]. <br> | |
- | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=J2J:5-O-[(S)-[(2,3-dihydroxybenzene-1-carbonyl)oxy](hydroxy)phosphoryl]adenosine'>J2J</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |
- | [[Category: | + | <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=6e97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e97 OCA], [http://pdbe.org/6e97 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e97 RCSB], [http://www.ebi.ac.uk/pdbsum/6e97 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e97 ProSAT]</span></td></tr> |
+ | </table> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Bruner, S D]] | ||
+ | [[Category: Zagulyaeva, A A]] | ||
+ | [[Category: Adenylation domain]] | ||
+ | [[Category: Dihydroxybenzoic acid activating enzyme]] | ||
+ | [[Category: Ligase]] | ||
+ | [[Category: Siderophore biosynthesis]] |
Revision as of 05:49, 21 August 2019
Implication of MbtH-like proteins in crystallization of the independent NRPS A domains. Crystal structure of FscC: supporting rationale for revised mechanism of freestanding aryl acid adenylating enzymes.
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