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.


4ijd

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (20:50, 16 November 2022) (edit) (undo)
 
(2 intermediate revisions not shown.)
Line 1: Line 1:
 +
==Crystal structure of methyltransferase domain of human PR domain-containing protein 9==
==Crystal structure of methyltransferase domain of human PR domain-containing protein 9==
-
<StructureSection load='4ijd' size='340' side='right' caption='[[4ijd]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
+
<StructureSection load='4ijd' size='340' side='right'caption='[[4ijd]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4ijd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IJD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IJD FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4ijd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IJD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IJD FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4ijd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ijd OCA], [https://pdbe.org/4ijd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ijd RCSB], [https://www.ebi.ac.uk/pdbsum/4ijd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ijd ProSAT]</span></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PRDM9, PFM6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
+
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </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=4ijd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ijd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ijd RCSB], [http://www.ebi.ac.uk/pdbsum/4ijd PDBsum]</span></td></tr>
+
</table>
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/PRDM9_HUMAN PRDM9_HUMAN] Histone methyltransferase that specifically trimethylates 'Lys-4' of histone H3 during meiotic prophase and is essential for proper meiotic progression. Does not have the ability to mono- and dimethylate 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Plays a central role in the transcriptional activation of genes during early meiotic prophase (By similarity).
==See Also==
==See Also==
-
*[[Histone methyltransferase|Histone methyltransferase]]
+
*[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Histone-lysine N-methyltransferase]]
 
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Arrowsmith, C H]]
+
[[Category: Large Structures]]
-
[[Category: Bountra, C]]
+
[[Category: Arrowsmith CH]]
-
[[Category: Brown, P J]]
+
[[Category: Bountra C]]
-
[[Category: Dombrovski, L]]
+
[[Category: Brown PJ]]
-
[[Category: Dong, A]]
+
[[Category: Dombrovski L]]
-
[[Category: Edwards, A M]]
+
[[Category: Dong A]]
-
[[Category: Li, Y]]
+
[[Category: Edwards AM]]
-
[[Category: Structural genomic]]
+
[[Category: Li Y]]
-
[[Category: Tempel, W]]
+
[[Category: Tempel W]]
-
[[Category: Wu, H]]
+
[[Category: Wu H]]
-
[[Category: Methyltransferase]]
+
-
[[Category: Prdm9]]
+
-
[[Category: Sgc]]
+
-
[[Category: Transferase]]
+

Current revision

Crystal structure of methyltransferase domain of human PR domain-containing protein 9

PDB ID 4ijd

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools