5efs: Difference between revisions
From Proteopedia
Jump to navigationJump to search
m Protected "5efs" [edit=sysop:move=sysop] |
No edit summary |
||
| Line 1: | Line 1: | ||
==The crystal structure of human kynurenine aminotransferase II== | ==The crystal structure of human kynurenine aminotransferase II== | ||
<StructureSection load='5efs' size='340' side='right' caption='[[5efs]], [[Resolution|resolution]] 1.83Å' scene=''> | <StructureSection load='5efs' size='340' side='right'caption='[[5efs]], [[Resolution|resolution]] 1.83Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5efs]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5efs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EFS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EFS FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.82503Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5efs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5efs OCA], [https://pdbe.org/5efs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5efs RCSB], [https://www.ebi.ac.uk/pdbsum/5efs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5efs ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/AADAT_HUMAN AADAT_HUMAN] Transaminase with broad substrate specificity. Has transaminase activity towards aminoadipate, kynurenine, methionine and glutamate. Shows activity also towards tryptophan, aspartate and hydroxykynurenine. Accepts a variety of oxo-acids as amino-group acceptors, with a preference for 2-oxoglutarate, 2-oxocaproic acid, phenylpyruvate and alpha-oxo-gamma-methiol butyric acid. Can also use glyoxylate as amino-group acceptor (in vitro).<ref>PMID:18620547</ref> | ||
==See Also== | |||
*[[Aminotransferase 3D structures|Aminotransferase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Church | [[Category: Large Structures]] | ||
[[Category: Hanrahan | [[Category: Church WB]] | ||
[[Category: Harrop | [[Category: Hanrahan JR]] | ||
[[Category: Kwan | [[Category: Harrop SJ]] | ||
[[Category: Nadvi | [[Category: Kwan A]] | ||
[[Category: Nematollahi | [[Category: Nadvi NA]] | ||
[[Category: Sun | [[Category: Nematollahi A]] | ||
[[Category: Sun G]] | |||