Ascorbate peroxidase
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
| - | The <scene name='48/486478/Cv/2'>heme-containing active site</scene> of APX contains a <scene name='48/486478/Cv/3'>His residue (H163 in soybean) which coordinates with the heme</scene> and confers stability to the Fe state in the heme. | + | The <scene name='48/486478/Cv/2'>heme-containing active site</scene> of APX contains a <scene name='48/486478/Cv/3'>His residue (H163 in soybean) which coordinates with the heme</scene> and confers stability to the Fe state in the heme. <ref>PMID:12640445</ref> |
</StructureSection> | </StructureSection> | ||
==3D structures of ascorbate peroxidase== | ==3D structures of ascorbate peroxidase== | ||
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**[[4ged]] – LmAPX + cytochrome c<br /> | **[[4ged]] – LmAPX + cytochrome c<br /> | ||
}} | }} | ||
| + | == References == | ||
| + | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 13:11, 9 November 2015
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3D structures of ascorbate peroxidase
Updated on 09-November-2015
References
- ↑ Sharp KH, Mewies M, Moody PC, Raven EL. Crystal structure of the ascorbate peroxidase-ascorbate complex. Nat Struct Biol. 2003 Apr;10(4):303-7. PMID:12640445 doi:http://dx.doi.org/10.1038/nsb913
