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1vll
From Proteopedia
(Difference between revisions)
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<StructureSection load='1vll' size='340' side='right'caption='[[1vll]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='1vll' size='340' side='right'caption='[[1vll]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1vll]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1vll]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus_DSM_4304 Archaeoglobus fulgidus DSM 4304]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VLL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VLL FirstGlance]. <br> |
| - | </td></tr> | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1vll FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vll OCA], [https://pdbe.org/1vll PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vll RCSB], [https://www.ebi.ac.uk/pdbsum/1vll PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vll ProSAT], [https://www.topsan.org/Proteins/JCSG/1vll TOPSAN]</span></td></tr> |
| - | + | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/ALADH_ARCFU ALADH_ARCFU] Catalyzes the NAD(+)-dependent oxidative deamination of L-alanine to pyruvate, and the reverse reaction, the reductive amination of pyruvate. Its physiological role is not known. Can not use NADP(+) instead of NAD(+) as a cosubstrate. In the deamination direction, can also efficiently use L-2-aminobutyrate as substrate. In the reductive amination direction, also exhibits high activity with 2-oxobutyrate and oxaloacetate as substrate. In contrast to bacterial homologs, does not exhibit any ornithine cyclodeaminase activity.[HAMAP-Rule:MF_00935]<ref>PMID:15516582</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Archaeoglobus fulgidus DSM 4304]] |
| - | + | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Structural genomic]] | ||
| - | [[Category: Af1665]] | ||
| - | [[Category: Jcsg]] | ||
| - | [[Category: Oxidoreductase]] | ||
| - | [[Category: PSI, Protein structure initiative]] | ||
Revision as of 06:41, 25 January 2023
Crystal structure of alanine dehydrogenase (AF1665) from Archaeoglobus fulgidus at 2.80 A resolution
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