4cl3: Difference between revisions
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{{STRUCTURE_4cl3| PDB=4cl3 | SCENE= }} | {{STRUCTURE_4cl3| PDB=4cl3 | SCENE= }} | ||
===1.70 A resolution structure of the malate dehydrogenase from Chloroflexus aurantiacus=== | ===1.70 A resolution structure of the malate dehydrogenase from Chloroflexus aurantiacus=== | ||
{{ | {{ABSTRACT_PUBMED_24600446}} | ||
==Function== | ==Function== | ||
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==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:024600446</ref><references group="xtra"/><references/> | ||
[[Category: Chloroflexus sp. y-400-fl]] | [[Category: Chloroflexus sp. y-400-fl]] | ||
[[Category: Malate dehydrogenase]] | [[Category: Malate dehydrogenase]] | ||
Revision as of 12:00, 19 March 2014
1.70 A resolution structure of the malate dehydrogenase from Chloroflexus aurantiacus1.70 A resolution structure of the malate dehydrogenase from Chloroflexus aurantiacus
Template:ABSTRACT PUBMED 24600446
FunctionFunction
[MDH_CHLSY] Catalyzes the reversible oxidation of malate to oxaloacetate (By similarity).
About this StructureAbout this Structure
4cl3 is a 2 chain structure with sequence from Chloroflexus sp. y-400-fl. This structure supersedes the now removed PDB entry 4bgt. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Talon R, Coquelle N, Madern D, Girard E. An experimental point of view on hydration/solvation in halophilic proteins. Front Microbiol. 2014 Feb 21;5:66. doi: 10.3389/fmicb.2014.00066. eCollection, 2014. PMID:24600446 doi:http://dx.doi.org/10.3389/fmicb.2014.00066