› 3c5v

X-ray diffraction
2Å resolution

PP2A-specific methylesterase apo form (PME)

Released:
DOI: 10.2210/pdb3c5v/pdb
PDB entry 3c5v coloured by chain, front view.
PDB entry 3c5v coloured by chain, side view.
PDB entry 3c5v coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural mechanism of demethylation and inactivation of protein phosphatase 2A.
Xing Y, Li Z, Chen Y, Stock JB, Jeffrey PD, Shi Y
Cell 133 154-63 (2008)
PMID: 18394995

Function and Biology Details

Reaction catalysed: 
[Phosphatase 2A protein]-leucine methyl ester + H(2)O = [phosphatase 2A protein]-leucine + methanol
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195260 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein phosphatase methylesterase 1 Chain: A
Molecule details ›
Chain: A
Length: 316 amino acids
Theoretical weight: 34.74 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Y570 (Residues: 39-386; Coverage: 82%)
Gene names: PME1, PP2593, PPME1, PRO0750
Sequence domains: Alpha/beta hydrolase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P3121
Unit cell:
a: 82.512Å b: 82.512Å c: 90.843Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.183 0.183 0.22
Expression system: Escherichia coli

Quick links

Citations

36 review citations

Serine/threonine phosphatases: mechanism through structure.
Shi Y. (2009)
35 more

4 mentions without citation

Carboxylic ester hydrolases: Classification and database derived from their primary, secondary, and tertiary structures.
Chen et al. (2016)
3 more