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2ycl
From Proteopedia
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[[Image:2ycl.png|left|200px]] | [[Image:2ycl.png|left|200px]] | ||
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{{STRUCTURE_2ycl| PDB=2ycl | SCENE= }} | {{STRUCTURE_2ycl| PDB=2ycl | SCENE= }} | ||
===COMPLETE STRUCTURE OF THE CORRINOID,IRON-SULFUR PROTEIN INCLUDING THE N-TERMINAL DOMAIN WITH A 4FE-4S CLUSTER=== | ===COMPLETE STRUCTURE OF THE CORRINOID,IRON-SULFUR PROTEIN INCLUDING THE N-TERMINAL DOMAIN WITH A 4FE-4S CLUSTER=== | ||
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| - | (as it appears on PubMed at http://www.pubmed.gov), where 21640123 is the PubMed ID number. | ||
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{{ABSTRACT_PUBMED_21640123}} | {{ABSTRACT_PUBMED_21640123}} | ||
==About this Structure== | ==About this Structure== | ||
| - | [[2ycl]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Carboxydothermus_hydrogenoformans Carboxydothermus hydrogenoformans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YCL OCA]. | + | [[2ycl]] is a 2 chain structure of [[Carbon monoxide dehydrogenase]] with sequence from [http://en.wikipedia.org/wiki/Carboxydothermus_hydrogenoformans Carboxydothermus hydrogenoformans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YCL OCA]. |
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| + | ==See Also== | ||
| + | *[[Acetyl-CoA synthase|Acetyl-CoA synthase]] | ||
| + | *[[Carbon monoxide dehydrogenase|Carbon monoxide dehydrogenase]] | ||
==Reference== | ==Reference== | ||
Revision as of 14:04, 27 July 2012
Contents |
COMPLETE STRUCTURE OF THE CORRINOID,IRON-SULFUR PROTEIN INCLUDING THE N-TERMINAL DOMAIN WITH A 4FE-4S CLUSTER
Template:ABSTRACT PUBMED 21640123
About this Structure
2ycl is a 2 chain structure of Carbon monoxide dehydrogenase with sequence from Carboxydothermus hydrogenoformans. Full crystallographic information is available from OCA.
See Also
Reference
- Goetzl S, Jeoung JH, Hennig SE, Dobbek H. Structural Basis for Electron and Methyl-Group Transfer in a Methyltransferase System Operating in the Reductive Acetyl-CoA Pathway. J Mol Biol. 2011 Aug 5;411(1):96-109. Epub 2011 May 27. PMID:21640123 doi:10.1016/j.jmb.2011.05.025
