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.


4gm9

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
==Crystal structure of human WD repeat domain 5 with compound MM-401==
==Crystal structure of human WD repeat domain 5 with compound MM-401==
-
<StructureSection load='4gm9' size='340' side='right' caption='[[4gm9]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+
<StructureSection load='4gm9' size='340' side='right'caption='[[4gm9]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4gm9]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GM9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GM9 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4gm9]] is a 4 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=4GM9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GM9 FirstGlance]. <br>
-
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=0XO:2-METHYL-D-LYSINE'>0XO</scene>, <scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene>, <scene name='pdbligand=ALQ:2-METHYL-PROPIONIC+ACID'>ALQ</scene>, <scene name='pdbligand=PG9:D-PHENYLGLYCINE'>PG9</scene></td></tr>
+
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0XO:2-METHYL-D-LYSINE'>0XO</scene>, <scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene>, <scene name='pdbligand=ALQ:2-METHYL-PROPIONIC+ACID'>ALQ</scene>, <scene name='pdbligand=PG9:D-PHENYLGLYCINE'>PG9</scene></td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4gm3|4gm3]], [[4gm8|4gm8]], [[4gmb|4gmb]]</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=4gm9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gm9 OCA], [https://pdbe.org/4gm9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gm9 RCSB], [https://www.ebi.ac.uk/pdbsum/4gm9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gm9 ProSAT]</span></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">WDR5, BIG3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4gm9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gm9 OCA], [http://pdbe.org/4gm9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gm9 RCSB], [http://www.ebi.ac.uk/pdbsum/4gm9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gm9 ProSAT]</span></td></tr>
+
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/WDR5_HUMAN WDR5_HUMAN]] Contributes to histone modification. May position the N-terminus of histone H3 for efficient trimethylation at 'Lys-4'. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. May regulate osteoblasts differentiation.<ref>PMID:19556245</ref> <ref>PMID:19103755</ref> <ref>PMID:20018852</ref> <ref>PMID:16600877</ref> <ref>PMID:16829960</ref>
+
[https://www.uniprot.org/uniprot/WDR5_HUMAN WDR5_HUMAN] Contributes to histone modification. May position the N-terminus of histone H3 for efficient trimethylation at 'Lys-4'. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. May regulate osteoblasts differentiation.<ref>PMID:19556245</ref> <ref>PMID:19103755</ref> <ref>PMID:20018852</ref> <ref>PMID:16600877</ref> <ref>PMID:16829960</ref>
 +
 
 +
==See Also==
 +
*[[WD-repeat protein 3D structures|WD-repeat protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Human]]
+
[[Category: Homo sapiens]]
-
[[Category: Bernard, D]]
+
[[Category: Large Structures]]
-
[[Category: Chen, Y]]
+
[[Category: Bernard D]]
-
[[Category: Dou, Y]]
+
[[Category: Chen Y]]
-
[[Category: Karatas, H]]
+
[[Category: Dou Y]]
-
[[Category: Lei, M]]
+
[[Category: Karatas H]]
-
[[Category: Liu, L]]
+
[[Category: Lei M]]
-
[[Category: Townsend, E C]]
+
[[Category: Liu L]]
-
[[Category: Wang, S]]
+
[[Category: Townsend EC]]
-
[[Category: Histone methyltransferase]]
+
[[Category: Wang S]]
-
[[Category: Mll1]]
+
-
[[Category: Transcription-transcription inhibitor complex]]
+
-
[[Category: Wd40]]
+

Revision as of 07:05, 26 October 2022

Crystal structure of human WD repeat domain 5 with compound MM-401

PDB ID 4gm9

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools