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1oe1
From Proteopedia
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{{STRUCTURE_1oe1| PDB=1oe1 | SCENE= }} | {{STRUCTURE_1oe1| PDB=1oe1 | SCENE= }} | ||
===ATOMIC RESOLUTION STRUCTURE OF THE WILDTYPE NATIVE NITRITE REDUCTASE FROM ALCALIGENES XYLOSOXIDANS=== | ===ATOMIC RESOLUTION STRUCTURE OF THE WILDTYPE NATIVE NITRITE REDUCTASE FROM ALCALIGENES XYLOSOXIDANS=== | ||
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{{ABSTRACT_PUBMED_12691751}} | {{ABSTRACT_PUBMED_12691751}} | ||
==About this Structure== | ==About this Structure== | ||
| - | + | [[1oe1]] is a 1 chain structure of [[Nitric reductase]] with sequence from [http://en.wikipedia.org/wiki/Achromobacter_xylosoxidans Achromobacter xylosoxidans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OE1 OCA]. | |
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| + | ==See Also== | ||
| + | *[[Nitric reductase|Nitric reductase]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:012691751</ref><ref group="xtra">PMID:019053252</ref><references group="xtra"/> |
[[Category: Achromobacter xylosoxidans]] | [[Category: Achromobacter xylosoxidans]] | ||
[[Category: Dodd, F E.]] | [[Category: Dodd, F E.]] | ||
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[[Category: Denitrification]] | [[Category: Denitrification]] | ||
[[Category: Nitrite reductase]] | [[Category: Nitrite reductase]] | ||
| - | + | [[Category: Reductase]] | |
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Revision as of 09:56, 27 July 2012
Contents |
ATOMIC RESOLUTION STRUCTURE OF THE WILDTYPE NATIVE NITRITE REDUCTASE FROM ALCALIGENES XYLOSOXIDANS
Template:ABSTRACT PUBMED 12691751
About this Structure
1oe1 is a 1 chain structure of Nitric reductase with sequence from Achromobacter xylosoxidans. Full crystallographic information is available from OCA.
See Also
Reference
- Ellis MJ, Dodd FE, Sawers G, Eady RR, Hasnain SS. Atomic resolution structures of native copper nitrite reductase from Alcaligenes xylosoxidans and the active site mutant Asp92Glu. J Mol Biol. 2003 Apr 25;328(2):429-38. PMID:12691751
- Hough MA, Eady RR, Hasnain SS. Identification of the proton channel to the active site type 2 Cu center of nitrite reductase: structural and enzymatic properties of the His254Phe and Asn90Ser mutants. Biochemistry. 2008 Dec 23;47(51):13547-53. PMID:19053252 doi:10.1021/bi801369y
