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1qd1

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1qd1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QD1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QD1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1qd1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QD1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QD1 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FON:N-{[4-({[(6R)-2-AMINO-5-FORMYL-4-OXO-1,4,5,6,7,8-HEXAHYDROPTERIDIN-6-YL]METHYL}AMINO)PHENYL]CARBONYL}-L-GLUTAMIC+ACID'>FON</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene><br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FON:N-{[4-({[(6R)-2-AMINO-5-FORMYL-4-OXO-1,4,5,6,7,8-HEXAHYDROPTERIDIN-6-YL]METHYL}AMINO)PHENYL]CARBONYL}-L-GLUTAMIC+ACID'>FON</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_formimidoyltransferase Glutamate formimidoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.5 2.1.2.5] </span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_formimidoyltransferase Glutamate formimidoyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.2.5 2.1.2.5] </span></td></tr>
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<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=1qd1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qd1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qd1 RCSB], [http://www.ebi.ac.uk/pdbsum/1qd1 PDBsum]</span></td></tr>
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<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=1qd1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qd1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qd1 RCSB], [http://www.ebi.ac.uk/pdbsum/1qd1 PDBsum]</span></td></tr>
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<table>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/FTCD_PIG FTCD_PIG]] Folate-dependent enzyme, that displays both transferase and deaminase activity. Serves to channel one-carbon units from formiminoglutamate to the folate pool. Binds and promotes bundling of vimentin filaments originating from the Golgi (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Glutamate formimidoyltransferase]]
[[Category: Glutamate formimidoyltransferase]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Kohls, D.]]
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[[Category: Kohls, D]]
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[[Category: MacKenzie, R E.]]
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[[Category: MacKenzie, R E]]
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[[Category: Purisima, E.]]
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[[Category: Purisima, E]]
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[[Category: Sulea, T.]]
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[[Category: Sulea, T]]
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[[Category: Vrielink, A.]]
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[[Category: Vrielink, A]]
[[Category: Alpha-beta-beta-alpha sandwich]]
[[Category: Alpha-beta-beta-alpha sandwich]]
[[Category: Electrostatically charged substrate tunnel]]
[[Category: Electrostatically charged substrate tunnel]]
[[Category: Functional dimer]]
[[Category: Functional dimer]]
[[Category: Transferase]]
[[Category: Transferase]]

Revision as of 17:47, 24 December 2014

THE CRYSTAL STRUCTURE OF THE FORMIMINOTRANSFERASE DOMAIN OF FORMIMINOTRANSFERASE-CYCLODEAMINASE.

1qd1, resolution 1.70Å

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