6jzz: Difference between revisions

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'''Unreleased structure'''


The entry 6jzz is ON HOLD  until Paper Publication
==The crystal structure of AAR-C294S in complex with ADO.==
 
<StructureSection load='6jzz' size='340' side='right'caption='[[6jzz]], [[Resolution|resolution]] 3.01&Aring;' scene=''>
Authors: Zhang, H.M., Li, M., Gao, Y.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[6jzz]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JZZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6JZZ FirstGlance]. <br>
Description: The crystal structure of AAR-C294S in complex with ADO.
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=PL3:HEXADECAN-1-OL'>PL3</scene>, <scene name='pdbligand=ST9:STEAROYL-COENZYME+A'>ST9</scene></td></tr>
[[Category: Unreleased Structures]]
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Long-chain_acyl-[acyl-carrier-protein]_reductase Long-chain acyl-[acyl-carrier-protein] reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.80 1.2.1.80] </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=6jzz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jzz OCA], [http://pdbe.org/6jzz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jzz RCSB], [http://www.ebi.ac.uk/pdbsum/6jzz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jzz ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/AAR_SYNE7 AAR_SYNE7]] Catalyzes the NADP-dependent reduction of long-chain acyl-ACP to the corresponding fatty aldehyde. Involved in the biosynthesis of alkanes, mainly heptadecane and pentadecane, by producing the fatty aldehydes used by aldehyde decarbonylase.<ref>PMID:20671186</ref>  [[http://www.uniprot.org/uniprot/Q8KPT4_SYNE7 Q8KPT4_SYNE7]] Catalyzes the decarbonylation of fatty aldehydes to alkanes.[HAMAP-Rule:MF_00931]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Gao, Y]]
[[Category: Gao, Y]]
[[Category: Zhang, H.M]]
[[Category: Li, M]]
[[Category: Li, M]]
[[Category: Zhang, H M]]
[[Category: Aldehyde]]
[[Category: Alkane]]
[[Category: Oxidoreductase-lyase complex]]
[[Category: Oxygenase]]
[[Category: Reductase]]

Revision as of 12:06, 1 April 2020

The crystal structure of AAR-C294S in complex with ADO.The crystal structure of AAR-C294S in complex with ADO.

Structural highlights

6jzz is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Activity:[acyl-carrier-protein_reductase Long-chain acyl-[acyl-carrier-protein] reductase], with EC number 1.2.1.80
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[AAR_SYNE7] Catalyzes the NADP-dependent reduction of long-chain acyl-ACP to the corresponding fatty aldehyde. Involved in the biosynthesis of alkanes, mainly heptadecane and pentadecane, by producing the fatty aldehydes used by aldehyde decarbonylase.[1] [Q8KPT4_SYNE7] Catalyzes the decarbonylation of fatty aldehydes to alkanes.[HAMAP-Rule:MF_00931]

References

  1. ↑ Schirmer A, Rude MA, Li X, Popova E, del Cardayre SB. Microbial biosynthesis of alkanes. Science. 2010 Jul 30;329(5991):559-62. doi: 10.1126/science.1187936. PMID:20671186 doi:10.1126/science.1187936

6jzz, resolution 3.01Å

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