2po5
From Proteopedia
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[[Image:2po5.png|left|200px]] | [[Image:2po5.png|left|200px]] | ||
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{{STRUCTURE_2po5| PDB=2po5 | SCENE= }} | {{STRUCTURE_2po5| PDB=2po5 | SCENE= }} | ||
===Crystal structure of human ferrochelatase mutant with His 263 replaced by Cys=== | ===Crystal structure of human ferrochelatase mutant with His 263 replaced by Cys=== | ||
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{{ABSTRACT_PUBMED_17567154}} | {{ABSTRACT_PUBMED_17567154}} | ||
==About this Structure== | ==About this Structure== | ||
[[2po5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PO5 OCA]. | [[2po5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PO5 OCA]. | ||
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| + | ==See Also== | ||
| + | *[[Ferrochelatase|Ferrochelatase]] | ||
==Reference== | ==Reference== | ||
| - | <ref group="xtra">PMID: | + | <ref group="xtra">PMID:017567154</ref><ref group="xtra">PMID:011175906</ref><ref group="xtra">PMID:010561552</ref><references group="xtra"/> |
[[Category: Ferrochelatase]] | [[Category: Ferrochelatase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: H263c]] | [[Category: H263c]] | ||
[[Category: Heme biosynthesis]] | [[Category: Heme biosynthesis]] | ||
| + | [[Category: Lyase]] | ||
[[Category: Mature length]] | [[Category: Mature length]] | ||
[[Category: Proteolytically processed mitochondrial inner membrane protein]] | [[Category: Proteolytically processed mitochondrial inner membrane protein]] | ||
[[Category: Protoheme]] | [[Category: Protoheme]] | ||
Revision as of 13:03, 30 January 2013
Contents |
Crystal structure of human ferrochelatase mutant with His 263 replaced by Cys
Template:ABSTRACT PUBMED 17567154
About this Structure
2po5 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See Also
Reference
- Dailey HA, Wu CK, Horanyi P, Medlock AE, Najahi-Missaoui W, Burden AE, Dailey TA, Rose J. Altered orientation of active site residues in variants of human ferrochelatase. Evidence for a hydrogen bond network involved in catalysis. Biochemistry. 2007 Jul 10;46(27):7973-9. Epub 2007 Jun 14. PMID:17567154 doi:10.1021/bi700151f
- Wu CK, Dailey HA, Rose JP, Burden A, Sellers VM, Wang BC. The 2.0 A structure of human ferrochelatase, the terminal enzyme of heme biosynthesis. Nat Struct Biol. 2001 Feb;8(2):156-60. PMID:11175906 doi:10.1038/84152
- Burden AE, Wu C, Dailey TA, Busch JL, Dhawan IK, Rose JP, Wang B, Dailey HA. Human ferrochelatase: crystallization, characterization of the [2Fe-2S] cluster and determination that the enzyme is a homodimer. Biochim Biophys Acta. 1999 Nov 16;1435(1-2):191-7. PMID:10561552
Categories: Ferrochelatase | Homo sapiens | Burden, A. | Dailey, H A. | Dailey, T A. | Horanyi, P. | Medlock, A E. | Najahi-Missaoui, A E.W. | Rose, J P. | Wu, C K. | Fe2s2 cluster | Ferro-lyase | H263c | Heme biosynthesis | Lyase | Mature length | Proteolytically processed mitochondrial inner membrane protein | Protoheme
