Ascorbate peroxidase
From Proteopedia
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The <scene name='48/486478/Cv/4'>heme-containing active site</scene> of APX contains a <scene name='48/486478/Cv/5'>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> | The <scene name='48/486478/Cv/4'>heme-containing active site</scene> of APX contains a <scene name='48/486478/Cv/5'>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> | ||
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| + | ==3D structures of ascorbate peroxidase== | ||
| + | [[Ascorbate peroxidase 3D structures]] | ||
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</StructureSection> | </StructureSection> | ||
==3D structures of ascorbate peroxidase== | ==3D structures of ascorbate peroxidase== | ||
Revision as of 08:43, 20 March 2019
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3D structures of ascorbate peroxidase
Updated on 20-March-2019
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
