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2yl2
From Proteopedia
(Difference between revisions)
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| - | == | + | |
| + | ==Crystal structure of human acetyl-CoA carboxylase 1, biotin carboxylase (BC) domain== | ||
<StructureSection load='2yl2' size='340' side='right' caption='[[2yl2]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='2yl2' size='340' side='right' caption='[[2yl2]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2yl2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2yl2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YL2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YL2 FirstGlance]. <br> |
| - | </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=2yl2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yl2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2yl2 RCSB], [http://www.ebi.ac.uk/pdbsum/2yl2 PDBsum]</span></td></tr> | + | </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=2yl2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yl2 OCA], [http://pdbe.org/2yl2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2yl2 RCSB], [http://www.ebi.ac.uk/pdbsum/2yl2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2yl2 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Disease == | == Disease == | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/ACACA_HUMAN ACACA_HUMAN]] Catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase.<ref>PMID:20952656</ref> | [[http://www.uniprot.org/uniprot/ACACA_HUMAN ACACA_HUMAN]] Catalyzes the rate-limiting reaction in the biogenesis of long-chain fatty acids. Carries out three functions: biotin carboxyl carrier protein, biotin carboxylase and carboxyltransferase.<ref>PMID:20952656</ref> | ||
| - | |||
| - | ==See Also== | ||
| - | *[[Biotin carboxylase|Biotin carboxylase]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Human]] |
[[Category: Arrowsmith, C H]] | [[Category: Arrowsmith, C H]] | ||
[[Category: Beltrami, A]] | [[Category: Beltrami, A]] | ||
[[Category: Bountra, C]] | [[Category: Bountra, C]] | ||
| - | [[Category: Delft, F | + | [[Category: Delft, F von]] |
[[Category: Edwards, A M]] | [[Category: Edwards, A M]] | ||
[[Category: Froese, D S]] | [[Category: Froese, D S]] | ||
Revision as of 19:10, 24 January 2018
Crystal structure of human acetyl-CoA carboxylase 1, biotin carboxylase (BC) domain
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Categories: Human | Arrowsmith, C H | Beltrami, A | Bountra, C | Delft, F von | Edwards, A M | Froese, D S | Krojer, T | Krysztofinska, E | Muniz, J R.C | Oppermann, U | Vollmar, M | Weigelt, J | Yue, W W | Ligase
