4o29

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m (Protected "4o29" [edit=sysop:move=sysop])
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'''Unreleased structure'''
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{{STRUCTURE_4o29| PDB=4o29 | SCENE= }}
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===PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE from Pyrobaculum aerophilum in COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE===
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The entry 4o29 is ON HOLD
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==Function==
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[[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).
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Authors: Sawaya, Michael R., Yeates, Todd O., Griffith, Scott C.
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==About this Structure==
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[[4o29]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4O29 OCA].
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Description: PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE from Pyrobaculum aerophilum in COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE
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[[Category: Griffith, S C.]]
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[[Category: Sawaya, M R.]]
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[[Category: Yeates, T O.]]
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[[Category: Protein repair isomerization]]
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[[Category: Rossmann methyltransferase]]
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[[Category: Transferase]]

Revision as of 08:28, 15 January 2014

Template:STRUCTURE 4o29

PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE from Pyrobaculum aerophilum in COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE

Function

[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).

About this Structure

4o29 is a 1 chain structure. Full crystallographic information is available from OCA.

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OCA

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