› 4o29

X-ray diffraction
2.9Å resolution

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

Released:
DOI: 10.2210/pdb4o29/pdb
PDB entry 4o29 coloured by chain, front view.
PDB entry 4o29 coloured by chain, side view.
PDB entry 4o29 coloured by chain, top view.
Source organism: Pyrobaculum aerophilum str. IM2
Primary publication:
Structure of L-isoaspartyl (D-aspartyl) Methyltransferase
Griffith SC
Thesis University of California, Los Angeles 93-107 (2002)

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + protein L-isoaspartate = S-adenosyl-L-homocysteine + protein L-isoaspartate alpha-methyl ester
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187435 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein-L-isoaspartate O-methyltransferase Chain: A
Molecule details ›
Chain: A
Length: 208 amino acids
Theoretical weight: 23.24 KDa
Source organism: Pyrobaculum aerophilum str. IM2
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8ZYN0 (Residues: 1-205; Coverage: 100%)
Gene names: PAE0701, pcm
Sequence domains: Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PCMT)
Structure domains: Vaccinia Virus protein VP39

Ligands and Environments


Cofactor: Ligand SAH 1 x SAH
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: C2
Unit cell:
a: 73.72Å b: 35.67Å c: 66.29Å
α: 90° β: 100.31° γ: 90°
R-values:
R R work R free
0.215 0.21 0.261
Expression system: Escherichia coli

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