3cn8: Difference between revisions

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<StructureSection load='3cn8' size='340' side='right' caption='[[3cn8]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='3cn8' size='340' side='right' caption='[[3cn8]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3cn8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CN8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CN8 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3cn8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CN8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CN8 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SPD:SPERMIDINE'>SPD</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SPD:SPERMIDINE'>SPD</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1rsg|1rsg]], [[1yy5|1yy5]], [[1xpq|1xpq]], [[3cnd|3cnd]], [[3cnp|3cnp]], [[3cns|3cns]], [[3cnt|3cnt]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1rsg|1rsg]], [[1yy5|1yy5]], [[1xpq|1xpq]], [[3cnd|3cnd]], [[3cnp|3cnp]], [[3cns|3cns]], [[3cnt|3cnt]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FMS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FMS1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.3.13, 1.5.3.14, 1.5.3.15, 1.5.3.16 and 1.5.3.17 1.5.3.13, 1.5.3.14, 1.5.3.15, 1.5.3.16 and 1.5.3.17] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.3.13, 1.5.3.14, 1.5.3.15, 1.5.3.16 and 1.5.3.17 1.5.3.13, 1.5.3.14, 1.5.3.15, 1.5.3.16 and 1.5.3.17] </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=3cn8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cn8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3cn8 RCSB], [http://www.ebi.ac.uk/pdbsum/3cn8 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=3cn8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cn8 OCA], [http://pdbe.org/3cn8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3cn8 RCSB], [http://www.ebi.ac.uk/pdbsum/3cn8 PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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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/chain_selection.php?pdb_ID=2ata ConSurf].
</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=3cn8 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>


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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Hao, Q]]
[[Category: Hao, Q]]
[[Category: Huang, Q]]
[[Category: Huang, Q]]

Revision as of 23:26, 7 February 2016

Crystal structure of fms1 in complex with spermidineCrystal structure of fms1 in complex with spermidine

Structural highlights

3cn8 is a 2 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Gene:FMS1 (ATCC 18824)
Activity:Oxidoreductase, with EC number 1.5.3.14, 1.5.3.15, 1.5.3.16 and 1.5.3.17 1.5.3.13, 1.5.3.14, 1.5.3.15, 1.5.3.16 and 1.5.3.17
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[FMS1_YEAST] Involved in the production of beta-alanine, a precursor of pantothenic acid. Multicopy suppressor of fenpropimorph resistance.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Landry J, Sternglanz R. Yeast Fms1 is a FAD-utilizing polyamine oxidase. Biochem Biophys Res Commun. 2003 Apr 11;303(3):771-6. PMID:12670477
  2. ↑ Chattopadhyay MK, Tabor CW, Tabor H. Spermidine but not spermine is essential for hypusine biosynthesis and growth in Saccharomyces cerevisiae: spermine is converted to spermidine in vivo by the FMS1-amine oxidase. Proc Natl Acad Sci U S A. 2003 Nov 25;100(24):13869-74. Epub 2003 Nov 14. PMID:14617780 doi:http://dx.doi.org/10.1073/pnas.1835918100

3cn8, resolution 2.40Å

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