4o9i
From Proteopedia
(Difference between revisions)
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<StructureSection load='4o9i' size='340' side='right' caption='[[4o9i]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='4o9i' size='340' side='right' caption='[[4o9i]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4o9i]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O9I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O9I FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4o9i]] is a 1 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=4O9I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4O9I FirstGlance]. <br> |
</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> | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CHD4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12] </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=4o9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o9i OCA], [http://pdbe.org/4o9i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o9i RCSB], [http://www.ebi.ac.uk/pdbsum/4o9i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o9i 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=4o9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o9i OCA], [http://pdbe.org/4o9i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4o9i RCSB], [http://www.ebi.ac.uk/pdbsum/4o9i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4o9i ProSAT]</span></td></tr> | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/CHD4_HUMAN CHD4_HUMAN]] Component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones.<ref>PMID:9804427</ref> <ref>PMID:17626165</ref> | [[http://www.uniprot.org/uniprot/CHD4_HUMAN CHD4_HUMAN]] Component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin by deacetylating histones.<ref>PMID:9804427</ref> <ref>PMID:17626165</ref> | ||
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| - | ==See Also== | ||
| - | *[[Chromodomain-helicase-DNA-binding protein|Chromodomain-helicase-DNA-binding protein]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: DNA helicase]] | [[Category: DNA helicase]] | ||
| + | [[Category: Human]] | ||
[[Category: Chruszcz, M]] | [[Category: Chruszcz, M]] | ||
[[Category: Khorasanizadeh, S]] | [[Category: Khorasanizadeh, S]] | ||
Revision as of 08:22, 22 November 2017
Structure of CHD4 double chromodomains depicts cooperative folding for DNA binding
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