3cbf
From Proteopedia
(Difference between revisions)
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<StructureSection load='3cbf' size='340' side='right' caption='[[3cbf]], [[Resolution|resolution]] 1.67Å' scene=''> | <StructureSection load='3cbf' size='340' side='right' caption='[[3cbf]], [[Resolution|resolution]] 1.67Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3cbf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3cbf]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CBF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CBF FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=N5F:(2S)-2-[({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)AMINO]HEXANEDIOIC+ACID'>N5F</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=N5F:(2S)-2-[({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)AMINO]HEXANEDIOIC+ACID'>N5F</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2dtv|2dtv]], [[2egy|2egy]], [[2z1y|2z1y]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2dtv|2dtv]], [[2egy|2egy]], [[2z1y|2z1y]]</td></tr> | ||
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lysN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lysN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 "Flavobacterium thermophilum" Yoshida and Oshima 1971])</td></tr> |
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2-aminoadipate_transaminase 2-aminoadipate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.39 2.6.1.39] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2-aminoadipate_transaminase 2-aminoadipate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.39 2.6.1.39] </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=3cbf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cbf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3cbf RCSB], [http://www.ebi.ac.uk/pdbsum/3cbf 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=3cbf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cbf OCA], [http://pdbe.org/3cbf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3cbf RCSB], [http://www.ebi.ac.uk/pdbsum/3cbf PDBsum]</span></td></tr> |
</table> | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/LYSN_THET2 LYSN_THET2]] Catalyzes the transfer of an amino group between 2-oxoadipate (2-OA) and glutamate (Glu) to yield alpha-aminodipate (AAA). It can also transaminate glutamate, leucine, and aromatic amino acids. It also contributes in the biosynthesis of other amino acids such as leucine.<ref>PMID:15256574</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
- | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3cbf ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
+ | <div class="pdbe-citations 3cbf" style="background-color:#fffaf0;"></div> | ||
+ | |||
+ | ==See Also== | ||
+ | *[[Aminotransferase|Aminotransferase]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
+ | [[Category: Flavobacterium thermophilum yoshida and oshima 1971]] | ||
[[Category: 2-aminoadipate transaminase]] | [[Category: 2-aminoadipate transaminase]] | ||
- | [[Category: Thermus thermophilus]] | ||
[[Category: Fushinobu, S]] | [[Category: Fushinobu, S]] | ||
[[Category: Kuzuyama, T]] | [[Category: Kuzuyama, T]] | ||
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[[Category: Alpha-aminoadipate aminotransferase]] | [[Category: Alpha-aminoadipate aminotransferase]] | ||
[[Category: Substrate specifity]] | [[Category: Substrate specifity]] | ||
+ | [[Category: Thermus thermophilus]] | ||
[[Category: Transferase]] | [[Category: Transferase]] |
Revision as of 07:25, 7 February 2016
Crystal structure of LysN, alpha-aminoadipate aminotransferase, from Thermus thermophilus HB27
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