5ynw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:24, 27 March 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='5ynw' size='340' side='right'caption='[[5ynw]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
<StructureSection load='5ynw' size='340' side='right'caption='[[5ynw]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5ynw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Fischerella_utex1903 Fischerella utex1903]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YNW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YNW FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5ynw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Fischerella_ambigua_UTEX_1903 Fischerella ambigua UTEX 1903]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YNW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YNW FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8XL:3-[(Z)-2-isocyanoethenyl]-1H-indole'>8XL</scene>, <scene name='pdbligand=DST:DIMETHYLALLYL+S-THIOLODIPHOSPHATE'>DST</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ynt|5ynt]], [[5ynv|5ynv]], [[5ynu|5ynu]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8XL:3-[(Z)-2-isocyanoethenyl]-1H-indole'>8XL</scene>, <scene name='pdbligand=DST:DIMETHYLALLYL+S-THIOLODIPHOSPHATE'>DST</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ambP3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=230521 Fischerella UTEX1903])</td></tr>
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ynw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ynw OCA], [https://pdbe.org/5ynw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ynw RCSB], [https://www.ebi.ac.uk/pdbsum/5ynw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ynw 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=5ynw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ynw OCA], [http://pdbe.org/5ynw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ynw RCSB], [http://www.ebi.ac.uk/pdbsum/5ynw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ynw ProSAT]</span></td></tr>
+
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/V5TDY7_FISAU V5TDY7_FISAU]
-
FamD1 is a novel CloQ/NphB-family indole prenyltransferase which involves in hapalindole-type alkaloid biosynthesis. Here the native FamD1 structure and three protein-ligand complexes are analyzed to investigate the molecular basis of substrate binding and catalysis. FamD1 adopts a typical ABBA architecture of aromatic prenyltransferase, in which the substrate-binding chamber is found in the central beta-barrel. The indole-containing acceptor substrate is bound adjacent to the prenyl donor. Based on the complex structures, a catalytic mechanism of FamD1 is proposed. Functional implications on the sister enzyme FamD2 are also discussed.
+
-
 
+
-
Structural insight into a novel indole prenyltransferase in hapalindole-type alkaloid biosynthesis.,Wang J, Chen CC, Yang Y, Liu W, Ko TP, Shang N, Hu X, Xie Y, Huang JW, Zhang Y, Guo RT Biochem Biophys Res Commun. 2018 Jan 8;495(2):1782-1788. doi:, 10.1016/j.bbrc.2017.12.039. Epub 2017 Dec 8. PMID:29229390<ref>PMID:29229390</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 5ynw" style="background-color:#fffaf0;"></div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Fischerella utex1903]]
+
[[Category: Fischerella ambigua UTEX 1903]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Chen, C C]]
+
[[Category: Chen CC]]
-
[[Category: Guo, R T]]
+
[[Category: Guo RT]]
-
[[Category: Liu, W D]]
+
[[Category: Liu WD]]
-
[[Category: Wang, J]]
+
[[Category: Wang J]]
-
[[Category: Prenyltransferase]]
+
-
[[Category: Transferase]]
+

Current revision

Crystal structure of an aromatic prenyltransferase FAMD1 from Fischerella ambigua UTEX 1903 in complex with DMASPP and INN

PDB ID 5ynw

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools