› 1i1n

X-ray diffraction
1.5Å resolution

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149513 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein-L-isoaspartate(D-aspartate) O-methyltransferase Chain: A
Molecule details ›
Chain: A
Length: 226 amino acids
Theoretical weight: 24.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P22061 (Residues: 2-227; Coverage: 100%)
Gene name: PCMT1
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: RIGAKU RU300
Spacegroup: P21
Unit cell:
a: 48.105Å b: 53.917Å c: 48.814Å
α: 90° β: 116.15° γ: 90°
R-values:
R R work R free
0.183 0.183 0.213
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Aging as war between chemical and biochemical processes: protein methylation and the recognition of age-damaged proteins for repair.
Clarke S. (2003)
10 other articles

13 mentions without citation

Many paths to methyltransfer: a chronicle of convergence.
Schubert et al. (2003)
12 more