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3mz6
From Proteopedia
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[[Image:3mz6.png|left|200px]] | [[Image:3mz6.png|left|200px]] | ||
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{{STRUCTURE_3mz6| PDB=3mz6 | SCENE= }} | {{STRUCTURE_3mz6| PDB=3mz6 | SCENE= }} | ||
===Crystal structure of D101L Fe2+ HDAC8 complexed with M344=== | ===Crystal structure of D101L Fe2+ HDAC8 complexed with M344=== | ||
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{{ABSTRACT_PUBMED_20545365}} | {{ABSTRACT_PUBMED_20545365}} | ||
==About this Structure== | ==About this Structure== | ||
| - | [[3mz6]] is a 1 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=3MZ6 OCA]. | + | [[3mz6]] is a 1 chain structure of [[Histone deacetylase]] 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=3MZ6 OCA]. |
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| + | ==See Also== | ||
| + | *[[Histone deacetylase|Histone deacetylase]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:020545365</ref><references group="xtra"/> |
[[Category: Histone deacetylase]] | [[Category: Histone deacetylase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: Fierke, C A.]] | [[Category: Fierke, C A.]] | ||
[[Category: Gattis, S G.]] | [[Category: Gattis, S G.]] | ||
| + | [[Category: Arginase-fold]] | ||
| + | [[Category: Ferrous]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Metallohydrolase]] | ||
Revision as of 21:03, 26 July 2012
Contents |
Crystal structure of D101L Fe2+ HDAC8 complexed with M344
Template:ABSTRACT PUBMED 20545365
About this Structure
3mz6 is a 1 chain structure of Histone deacetylase with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Dowling DP, Gattis SG, Fierke CA, Christianson DW. Structures of metal-substituted human histone deacetylase 8 provide mechanistic inferences on biological function . Biochemistry. 2010 Jun 22;49(24):5048-56. PMID:20545365 doi:10.1021/bi1005046
