2psw: Difference between revisions

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<StructureSection load='2psw' size='340' side='right'caption='[[2psw]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='2psw' size='340' side='right'caption='[[2psw]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2psw]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PSW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PSW FirstGlance]. <br>
<table><tr><td colspan='2'>[[2psw]] is a 3 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=2PSW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PSW FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2ob0|2ob0]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NAT13, MAK3, NAT5 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peptide_alpha-N-acetyltransferase Peptide alpha-N-acetyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.88 2.3.1.88] </span></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=2psw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2psw OCA], [https://pdbe.org/2psw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2psw RCSB], [https://www.ebi.ac.uk/pdbsum/2psw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2psw ProSAT]</span></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=2psw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2psw OCA], [https://pdbe.org/2psw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2psw RCSB], [https://www.ebi.ac.uk/pdbsum/2psw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2psw ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/NAA50_HUMAN NAA50_HUMAN]] Probable catalytic component of the NAA11-NAA15 complex which displays alpha (N-terminal) acetyltransferase activity.<ref>PMID:16507339</ref>
[https://www.uniprot.org/uniprot/NAA50_HUMAN NAA50_HUMAN] Probable catalytic component of the NAA11-NAA15 complex which displays alpha (N-terminal) acetyltransferase activity.<ref>PMID:16507339</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: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Peptide alpha-N-acetyltransferase]]
[[Category: Antoshenko T]]
[[Category: Antoshenko, T]]
[[Category: Arrowsmith CH]]
[[Category: Arrowsmith, C H]]
[[Category: Bernstein G]]
[[Category: Bernstein, G]]
[[Category: Bochkarev A]]
[[Category: Bochkarev, A]]
[[Category: Edwards AM]]
[[Category: Edwards, A M]]
[[Category: Loppnau P]]
[[Category: Loppnau, P]]
[[Category: Plotnikov AN]]
[[Category: Plotnikov, A N]]
[[Category: Schuetz A]]
[[Category: Structural genomic]]
[[Category: Sundstrom M]]
[[Category: Schuetz, A]]
[[Category: Walker JR]]
[[Category: Sundstrom, M]]
[[Category: Weigelt J]]
[[Category: Walker, J R]]
[[Category: Wu H]]
[[Category: Weigelt, J]]
[[Category: Wu, H]]
[[Category: Acetyltransferase]]
[[Category: Sgc]]
[[Category: Transferase]]

Revision as of 14:08, 30 August 2023

Human MAK3 homolog in complex with CoAHuman MAK3 homolog in complex with CoA

Structural highlights

2psw is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NAA50_HUMAN Probable catalytic component of the NAA11-NAA15 complex which displays alpha (N-terminal) acetyltransferase activity.[1]

Evolutionary Conservation

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

References

  1. ↑ Arnesen T, Anderson D, Torsvik J, Halseth HB, Varhaug JE, Lillehaug JR. Cloning and characterization of hNAT5/hSAN: an evolutionarily conserved component of the NatA protein N-alpha-acetyltransferase complex. Gene. 2006 Apr 26;371(2):291-5. Epub 2006 Feb 28. PMID:16507339 doi:http://dx.doi.org/S0378-1119(05)00749-3

2psw, resolution 2.10Å

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