1s4d: Difference between revisions

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<StructureSection load='1s4d' size='340' side='right'caption='[[1s4d]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='1s4d' size='340' side='right'caption='[[1s4d]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1s4d]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/"pseudomonas_denitrificans"_(christensen_1903)_bergey_et_al._1923,_nom._rejic. "pseudomonas denitrificans" (christensen 1903) bergey et al. 1923, nom. rejic.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S4D OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1S4D FirstGlance]. <br>
<table><tr><td colspan='2'>[[1s4d]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_denitrificans_(nom._rej.) Pseudomonas denitrificans (nom. rej.)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S4D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S4D FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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]] 2.7&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">COBA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=43306 "Pseudomonas denitrificans" (Christensen 1903) Bergey et al. 1923, nom. rejic.])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Uroporphyrinogen-III_C-methyltransferase Uroporphyrinogen-III C-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.107 2.1.1.107] </span></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=1s4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s4d OCA], [https://pdbe.org/1s4d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s4d RCSB], [https://www.ebi.ac.uk/pdbsum/1s4d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s4d ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1s4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s4d OCA], [http://pdbe.org/1s4d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1s4d RCSB], [http://www.ebi.ac.uk/pdbsum/1s4d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1s4d ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/SUMT_PSEDE SUMT_PSEDE]] Catalyzes the methylation of both C-2 and C-7 of uroporphyrinogen III leading to precorrin-1 and precorrin-2; their oxidative esterification gives respectively factor I octamethyl ester and sirohydrochlorin.  
[https://www.uniprot.org/uniprot/SUMT_SINSX SUMT_SINSX] Catalyzes the two successive C-2 and C-7 methylation reactions involved in the conversion of uroporphyrinogen III to precorrin-2 via the intermediate formation of precorrin-1. It is a step in the biosynthesis of both cobalamin (vitamin B12) and siroheme. Neither uroporphyrin III nor the chlorin (factor I) is a substrate of SUMT.<ref>PMID:2546914</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Uroporphyrinogen-III C-methyltransferase]]
[[Category: Brindley AA]]
[[Category: Brindley, A A]]
[[Category: Getzoff ED]]
[[Category: Getzoff, E D]]
[[Category: Graham RM]]
[[Category: Graham, R M]]
[[Category: Raux E]]
[[Category: Raux, E]]
[[Category: Roessner CA]]
[[Category: Roessner, C A]]
[[Category: Roper DI]]
[[Category: Roper, D I]]
[[Category: Schubert HL]]
[[Category: Schubert, H L]]
[[Category: Scott AI]]
[[Category: Scott, A I]]
[[Category: Stamford NPJ]]
[[Category: Stamford, N P.J]]
[[Category: Stroupe ME]]
[[Category: Stroupe, M E]]
[[Category: Vevodova J]]
[[Category: Vevodova, J]]
[[Category: Warren MJ]]
[[Category: Warren, M J]]
[[Category: Wilson KS]]
[[Category: Wilson, K S]]
[[Category: Cobalamin]]
[[Category: Sah]]
[[Category: Sam]]
[[Category: Tetrapyrrole biosynthesis]]
[[Category: Transferase]]
[[Category: Uroporphyrinogen-iii methyltransferase]]

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