Arsenate reductase
From Proteopedia
(Difference between revisions)
| Line 27: | Line 27: | ||
**[[1i9d]] – EcAsR – ''Escherichia coli'' <BR /> | **[[1i9d]] – EcAsR – ''Escherichia coli'' <BR /> | ||
**[[1s3c]], [[1s3d]], [[1sd8]], [[1sd9]], [[1sk2]] – EcAsR (mutant) <BR /> | **[[1s3c]], [[1s3d]], [[1sd8]], [[1sd9]], [[1sk2]] – EcAsR (mutant) <BR /> | ||
| - | **[[2l17]], [[2l18], [[2myn]], [[2myp]] – SyAsR – ''Synechocystis'' - NMR<BR /> | + | **[[2l17]], [[2l18]], [[2myn]], [[2myp]] – SyAsR – ''Synechocystis'' - NMR<BR /> |
**[[2l19]], [[2myt]], [[2myu]] – SyAsR (mutant) - NMR<BR /> | **[[2l19]], [[2myt]], [[2myu]] – SyAsR (mutant) - NMR<BR /> | ||
**[[1y1l]] – AsR – ''Archaeoglobus fulgidus''<br /> | **[[1y1l]] – AsR – ''Archaeoglobus fulgidus''<br /> | ||
Revision as of 10:02, 9 March 2017
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3D structures of arsenate reductase
Updated on 09-March-2017
References
- ↑ Holmgren A, Aslund F. Glutaredoxin. Methods Enzymol. 1995;252:283-92. PMID:7476363
- ↑ Martin P, DeMel S, Shi J, Gladysheva T, Gatti DL, Rosen BP, Edwards BF. Insights into the structure, solvation, and mechanism of ArsC arsenate reductase, a novel arsenic detoxification enzyme. Structure. 2001 Nov;9(11):1071-81. PMID:11709171
