This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


4pin

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:17, 27 September 2023) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
 +
==Ergothioneine-biosynthetic methyltransferase EgtD in complex with N,N-dimethylhistidine==
==Ergothioneine-biosynthetic methyltransferase EgtD in complex with N,N-dimethylhistidine==
-
<StructureSection load='4pin' size='340' side='right' caption='[[4pin]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+
<StructureSection load='4pin' size='340' side='right'caption='[[4pin]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4pin]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PIN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4PIN FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4pin]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis Mycolicibacterium smegmatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PIN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PIN FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AVI:N,N-DIMETHYL-L-HISTIDINE'>AVI</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 1.9&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4pim|4pim]], [[4pio|4pio]], [[4pip|4pip]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AVI:N,N-DIMETHYL-L-HISTIDINE'>AVI</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-histidine_N(alpha)-methyltransferase L-histidine N(alpha)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.44 2.1.1.44] </span></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=4pin FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pin OCA], [https://pdbe.org/4pin PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pin RCSB], [https://www.ebi.ac.uk/pdbsum/4pin PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pin 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=4pin FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pin OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pin RCSB], [http://www.ebi.ac.uk/pdbsum/4pin PDBsum]</span></td></tr>
+
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/EGTD_MYCS2 EGTD_MYCS2]] Catalyzes the methylations of histidine to form N-alpha,N-alpha,N-alpha-trimethyl-L-histidine (also known as hercynine). Histidine and alpha-N,N-dimethylhistidine are preferred substrates.<ref>PMID:20420449</ref>
+
[https://www.uniprot.org/uniprot/EGTD_MYCS2 EGTD_MYCS2] Catalyzes the methylations of histidine to form N-alpha,N-alpha,N-alpha-trimethyl-L-histidine (also known as hercynine). Histidine and alpha-N,N-dimethylhistidine are preferred substrates.<ref>PMID:20420449</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 18: Line 18:
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
 +
<div class="pdbe-citations 4pin" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Blankenfeldt, W]]
+
[[Category: Large Structures]]
-
[[Category: Seebeck, F P]]
+
[[Category: Mycolicibacterium smegmatis]]
-
[[Category: Vit, A]]
+
[[Category: Blankenfeldt W]]
-
[[Category: Ergothioneine]]
+
[[Category: Seebeck FP]]
-
[[Category: Histidine betaine]]
+
[[Category: Vit A]]
-
[[Category: Methyltransferase]]
+
-
[[Category: Transferase]]
+

Current revision

Ergothioneine-biosynthetic methyltransferase EgtD in complex with N,N-dimethylhistidine

PDB ID 4pin

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools