4o29

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

Structural highlights

4o29 is a 1 chain structure with sequence from Pyrobaculum aerophilum str. IM2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.9Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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).

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OCA

4o29

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

Structural highlights

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4o29

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

Structural highlights

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