4o29: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
(4 intermediate revisions by the same user not shown)
Line 1: Line 1:
{{STRUCTURE_4o29|  PDB=4o29  |  SCENE=  }}
===PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE from Pyrobaculum aerophilum in COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE===


==Function==
==PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE from Pyrobaculum aerophilum in COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE==
[[http://www.uniprot.org/uniprot/PIMT_PYRAE PIMT_PYRAE]] Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins (By similarity).  
<StructureSection load='4o29' size='340' side='right'caption='[[4o29]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[4o29]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrobaculum_aerophilum_str._IM2 Pyrobaculum aerophilum str. IM2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O29 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4O29 FirstGlance]. <br>
[[4o29]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O29 OCA].
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
[[Category: Griffith, S C.]]
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
[[Category: Sawaya, M R.]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4o29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o29 OCA], [https://pdbe.org/4o29 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4o29 RCSB], [https://www.ebi.ac.uk/pdbsum/4o29 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4o29 ProSAT]</span></td></tr>
[[Category: Yeates, T O.]]
</table>
[[Category: Protein repair isomerization]]
== Function ==
[[Category: Rossmann methyltransferase]]
[https://www.uniprot.org/uniprot/PIMT_PYRAE PIMT_PYRAE] Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins (By similarity).
[[Category: Transferase]]
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pyrobaculum aerophilum str. IM2]]
[[Category: Griffith SC]]
[[Category: Sawaya MR]]
[[Category: Yeates TO]]