1rjg

X-ray diffraction
2.61Å resolution

Structure of PPM1, a leucine carboxy methyltransferase involved in the regulation of protein phosphatase 2A activity

Released:

Function and Biology Details

Reaction catalysed:
S-adenosyl-L-methionine + [phosphatase 2A protein]-leucine = S-adenosyl-L-homocysteine + [phosphatase 2A protein]-leucine methyl ester

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-169993 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Leucine carboxyl methyltransferase 1 Chain: A
Molecule details ›
Chain: A
Length: 334 amino acids
Theoretical weight: 38.57 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q04081 (Residues: 1-328; Coverage: 100%)
Gene names: PPM1, YDR435C
Sequence domains: Leucine carboxyl methyltransferase
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
Spacegroup: P212121
Unit cell:
a: 46.837Å b: 74.098Å c: 85.24Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.181 0.289
Expression system: Escherichia coli