4wd3

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<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=4wd3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wd3 OCA], [http://pdbe.org/4wd3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wd3 RCSB], [http://www.ebi.ac.uk/pdbsum/4wd3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wd3 ProSAT]</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=4wd3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wd3 OCA], [http://pdbe.org/4wd3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wd3 RCSB], [http://www.ebi.ac.uk/pdbsum/4wd3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wd3 ProSAT]</span></td></tr>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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RizA is an L-amino-acid ligase from Bacillus subtilis that participates in the biosynthesis of rhizocticin, an oligopeptide antibiotic. The substrate-free form of RizA has been crystallized and the structure was solved at 2.8 A resolution. The amino-acid-binding site appears to be capable of accommodating multiple amino acids, consistent with previous biochemical studies.
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Structure of RizA, an L-amino-acid ligase from Bacillus subtilis.,Kagawa W, Arai T, Ishikura S, Kino K, Kurumizaka H Acta Crystallogr F Struct Biol Commun. 2015 Sep;71(Pt 9):1125-30. doi:, 10.1107/S2053230X15012698. Epub 2015 Aug 25. PMID:26323296<ref>PMID:26323296</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4wd3" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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</StructureSection>
</StructureSection>

Revision as of 08:44, 1 January 2020

Crystal structure of an L-amino acid ligase RizA

PDB ID 4wd3

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