This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2vun
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2vun]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Eubacterium_barkeri Eubacterium barkeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VUN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VUN FirstGlance]. <br> | <table><tr><td colspan='2'>[[2vun]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Eubacterium_barkeri Eubacterium barkeri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VUN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VUN FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Enamidase Enamidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.18 3.5.2.18] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Enamidase Enamidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.18 3.5.2.18] </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=2vun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vun OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vun RCSB], [http://www.ebi.ac.uk/pdbsum/2vun 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=2vun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vun OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vun RCSB], [http://www.ebi.ac.uk/pdbsum/2vun PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/Q0QLE9_EUBBA Q0QLE9_EUBBA]] Decyclization of 6-oxo-1,4,5,6-tetrahydronicotinate to form 2-(enamine)glutarate, followed by hydrolysis to form (S)-2-formylglutarate.<ref>PMID:16894175</ref> <ref>PMID:18805424</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 31: | Line 33: | ||
[[Category: Enamidase]] | [[Category: Enamidase]] | ||
[[Category: Eubacterium barkeri]] | [[Category: Eubacterium barkeri]] | ||
| - | [[Category: Alhapel, A | + | [[Category: Alhapel, A]] |
| - | [[Category: Essen, L O | + | [[Category: Essen, L O]] |
| - | [[Category: Kress, D | + | [[Category: Kress, D]] |
| - | [[Category: Pierik, A J | + | [[Category: Pierik, A J]] |
[[Category: Amidohydrolase]] | [[Category: Amidohydrolase]] | ||
[[Category: Binuclear metal center]] | [[Category: Binuclear metal center]] | ||
Revision as of 11:13, 25 December 2014
THE CRYSTAL STRUCTURE OF ENAMIDASE AT 1.9 A RESOLUTION - A NEW MEMBER OF THE AMIDOHYDROLASE SUPERFAMILY
| |||||||||||
