4l5z

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 3: Line 3:
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4l5z]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Canal Canal]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L5Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4L5Z FirstGlance]. <br>
<table><tr><td colspan='2'>[[4l5z]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Canal Canal]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L5Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4L5Z FirstGlance]. <br>
-
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HCS:2-AMINO-4-MERCAPTO-BUTYRIC+ACID'>HCS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
+
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HCS:2-AMINO-4-MERCAPTO-BUTYRIC+ACID'>HCS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4l61|4l61]], [[4l64|4l64]], [[4l65|4l65]], [[4l6h|4l6h]], [[4l6o|4l6o]]</td></tr>
+
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4l61|4l61]], [[4l64|4l64]], [[4l65|4l65]], [[4l6h|4l6h]], [[4l6o|4l6o]]</td></tr>
-
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CaO19.10083, CaO19.2551, MET6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=237561 CANAL])</td></tr>
+
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CaO19.10083, CaO19.2551, MET6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=237561 CANAL])</td></tr>
-
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/5-methyltetrahydropteroyltriglutamate--homocysteine_S-methyltransferase 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.14 2.1.1.14] </span></td></tr>
+
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/5-methyltetrahydropteroyltriglutamate--homocysteine_S-methyltransferase 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.14 2.1.1.14] </span></td></tr>
-
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4l5z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l5z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4l5z RCSB], [http://www.ebi.ac.uk/pdbsum/4l5z PDBsum]</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=4l5z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l5z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4l5z RCSB], [http://www.ebi.ac.uk/pdbsum/4l5z PDBsum]</span></td></tr>
-
<table>
+
</table>
 +
== Function ==
 +
[[http://www.uniprot.org/uniprot/METE_CANAL METE_CANAL]] Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.[HAMAP-Rule:MF_00172]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 15: Line 17:
Structural analysis of a fungal methionine synthase with substrates and inhibitors.,Ubhi D, Kago G, Monzingo AF, Robertus JD J Mol Biol. 2014 Apr 17;426(8):1839-47. doi: 10.1016/j.jmb.2014.02.006. Epub 2014, Feb 11. PMID:24524835<ref>PMID:24524835</ref>
Structural analysis of a fungal methionine synthase with substrates and inhibitors.,Ubhi D, Kago G, Monzingo AF, Robertus JD J Mol Biol. 2014 Apr 17;426(8):1839-47. doi: 10.1016/j.jmb.2014.02.006. Epub 2014, Feb 11. PMID:24524835<ref>PMID:24524835</ref>
-
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
== References ==
== References ==
Line 23: Line 25:
[[Category: 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase]]
[[Category: 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase]]
[[Category: Canal]]
[[Category: Canal]]
-
[[Category: Robertus, J D.]]
+
[[Category: Robertus, J D]]
-
[[Category: Ubhi, D.]]
+
[[Category: Ubhi, D]]
[[Category: Cobalamin-independent]]
[[Category: Cobalamin-independent]]
[[Category: Dual tim barrel]]
[[Category: Dual tim barrel]]

Revision as of 06:33, 25 December 2014

Crystal structure of the Candida albicans Methionine Synthase in complex with Homocysteine

4l5z, resolution 2.18Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools