› 1r18

X-ray diffraction
2.2Å resolution

Drosophila protein isoaspartyl methyltransferase with S-adenosyl-L-homocysteine

Released:
DOI: 10.2210/pdb1r18/pdb
PDB entry 1r18 coloured by chain, front view.
PDB entry 1r18 coloured by chain, side view.
PDB entry 1r18 coloured by chain, top view.
Source organism: Drosophila melanogaster
Primary publication:
Catalytic implications from the Drosophila protein L-isoaspartyl methyltransferase structure and site-directed mutagenesis.
Bennett EJ, Bjerregaard J, Knapp JE, Chavous DA, Friedman AM, Royer WE, O'Connor CM
Biochemistry 42 12844-53 (2003)
PMID: 14596598

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

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-173287 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein-L-isoaspartate(D-aspartate) O-methyltransferase Chain: A
Molecule details ›
Chain: A
Length: 227 amino acids
Theoretical weight: 24.6 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q27869 (Residues: 1-221; Coverage: 98%)
Gene names: CG2152, PIAM, Pcmt
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: C2
Unit cell:
a: 72.07Å b: 45.25Å c: 61.24Å
α: 90° β: 102.9° γ: 90°
R-values:
R R work R free
0.203 0.194 0.233
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 citation in other articles

Substrates of the Arabidopsis thaliana protein isoaspartyl methyltransferase 1 identified using phage display and biopanning.
Chen et al. (2010)
6 more

2 mentions without citation

Combining specificity determining and conserved residues improves functional site prediction.
Kalinina et al. (2009)
1 more