1c9e
From Proteopedia
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- | [[Image:1c9e.png|left|200px]] | ||
- | + | ==STRUCTURE OF FERROCHELATASE WITH COPPER(II) N-METHYLMESOPORPHYRIN COMPLEX BOUND AT THE ACTIVE SITE== | |
+ | <StructureSection load='1c9e' size='340' side='right'caption='[[1c9e]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[1c9e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C9E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C9E FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MP1:N-METHYLMESOPORPHYRIN+CONTAINING+COPPER'>MP1</scene></td></tr> | ||
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1c9e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c9e OCA], [https://pdbe.org/1c9e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c9e RCSB], [https://www.ebi.ac.uk/pdbsum/1c9e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c9e ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/CPFC_BACSU CPFC_BACSU] Involved in coproporphyrin-dependent heme b biosynthesis (PubMed:25646457, PubMed:25908396). Catalyzes the insertion of ferrous iron into coproporphyrin III to form Fe-coproporphyrin III (PubMed:25646457, PubMed:25908396). It can also insert iron into protoporphyrin IX (PubMed:1459957, PubMed:8119288, PubMed:21052751, PubMed:25646457). Has weaker activity with 2,4 disulfonate, deuteroporphyrin and 2,4 hydroxyethyl (PubMed:25646457, PubMed:12761666). In vitro, can also use Zn(2+) or Cu(2+) (PubMed:8119288, PubMed:16140324, PubMed:21052751, PubMed:12761666).<ref>PMID:12761666</ref> <ref>PMID:1459957</ref> <ref>PMID:16140324</ref> <ref>PMID:21052751</ref> <ref>PMID:25646457</ref> <ref>PMID:25826316</ref> <ref>PMID:25908396</ref> <ref>PMID:8119288</ref> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c9/1c9e_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1c9e ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
- | == | + | ==See Also== |
- | + | *[[Ferrochelatase 3D structures|Ferrochelatase 3D structures]] | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | [[ | + | </StructureSection> |
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- | == | + | |
- | < | + | |
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: Al-Karadaghi | + | [[Category: Al-Karadaghi S]] |
- | [[Category: Fodje | + | [[Category: Fodje MN]] |
- | [[Category: Hansson | + | [[Category: Hansson A]] |
- | [[Category: Hansson | + | [[Category: Hansson M]] |
- | [[Category: Lecerof | + | [[Category: Lecerof D]] |
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Current revision
STRUCTURE OF FERROCHELATASE WITH COPPER(II) N-METHYLMESOPORPHYRIN COMPLEX BOUND AT THE ACTIVE SITE
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