2rml
From Proteopedia
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{{STRUCTURE_2rml| PDB=2rml | SCENE= }} | {{STRUCTURE_2rml| PDB=2rml | SCENE= }} | ||
- | + | ===Solution structure of the N-terminal soluble domains of Bacillus subtilis CopA=== | |
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- | + | The line below this paragraph, {{ABSTRACT_PUBMED_18215122}}, adds the Publication Abstract to the page | |
+ | (as it appears on PubMed at http://www.pubmed.gov), where 18215122 is the PubMed ID number. | ||
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==About this Structure== | ==About this Structure== | ||
- | 2RML is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full | + | 2RML is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RML OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Transmembrane]] | [[Category: Transmembrane]] | ||
[[Category: Transport]] | [[Category: Transport]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
+ | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 22:21:26 2008'' |
Revision as of 19:22, 28 July 2008
Solution structure of the N-terminal soluble domains of Bacillus subtilis CopA
Template:ABSTRACT PUBMED 18215122
About this Structure
2RML is a Single protein structure of sequence from Bacillus subtilis. Full experimental information is available from OCA.
Reference
Structure and Cu(I)-binding properties of the N-terminal soluble domains of Bacillus subtilis CopA., Singleton C, Banci L, Ciofi-Baffoni S, Tenori L, Kihlken M, Boetzel R, Le Brun N, Biochem J. 2008 Jan 23;. PMID:18215122
Page seeded by OCA on Mon Jul 28 22:21:26 2008
Categories: Bacillus subtilis | Single protein | Banci, L. | Bertini, I. | Boetzel, R. | Brun, N E.Le. | Ciofi-Baffoni, S. | Kihlken, M A. | Singleton, C. | Tenori, L. | Atp-binding | Copa | Copper | Copper transport | Hydrolase | Ion transport | Magnesium | Membrane | Metal-binding | Nucleotide-binding | P-type atpase | Phosphorylation | Transmembrane | Transport