3mif: Difference between revisions

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 ==Oxidized (Cu2+) peptidylglycine alpha-hydroxylating monooxygenase (PHM) with bound carbon monooxide (CO)==
-<StructureSection load='3mif' size='340' side='right' caption='[[3mif]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='3mif' size='340' side='right'caption='[[3mif]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3mif]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MIF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MIF FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3mif]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MIF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MIF FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
+</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&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1phm|1phm]], [[3mib|3mib]], [[3mic|3mic]], [[3mid|3mid]], [[3mie|3mie]], [[3mig|3mig]], [[3mih|3mih]], [[3mlj|3mlj]], [[3mlk|3mlk]], [[3mll|3mll]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Pam ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</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=3mif FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mif OCA], [https://pdbe.org/3mif PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mif RCSB], [https://www.ebi.ac.uk/pdbsum/3mif PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mif ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylglycine_monooxygenase Peptidylglycine monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.17.3 1.14.17.3] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3mif FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mif OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mif RCSB], [http://www.ebi.ac.uk/pdbsum/3mif PDBsum]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/AMD_RAT AMD_RAT] Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3mif" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Monooxygenase 3D structures|Monooxygenase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Peptidylglycine monooxygenase]]
+[[Category: Large Structures]]
 [[Category: Rattus norvegicus]]
-[[Category: Amzel, L M]]
+[[Category: Amzel LM]]
-[[Category: Chufan, E]]
+[[Category: Chufan E]]
-[[Category: Eipper, B A]]
+[[Category: Eipper BA]]
-[[Category: Mains, R E]]
+[[Category: Mains RE]]
-[[Category: Siebert, X]]
+[[Category: Siebert X]]
-[[Category: Ascorbate]]
-[[Category: Bioactive peptide activation]]
-[[Category: Monooxygenase]]
-[[Category: Oxidoreductase]]