2cm1

X-ray diffraction
2Å resolution

Crystal structure of the catalytic domain of serine threonine protein phosphatase PstP in complex with 2 Manganese ions.

Released:

Function and Biology Details

Reaction catalysed:
[a protein]-serine/threonine phosphate + H(2)O = [a protein]-serine/threonine + phosphate
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-161595 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine protein phosphatase PstP Chain: A
Molecule details ›
Chain: A
Length: 260 amino acids
Theoretical weight: 27.63 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WHW5 (Residues: 1-240; Coverage: 47%)
Gene names: Rv0018c, mstp, ppp, pstP
Sequence domains: Protein phosphatase 2C
Structure domains: PPM-type phosphatase domain

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P3221
Unit cell:
a: 69.142Å b: 69.142Å c: 89.431Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.199 0.197 0.243
Expression system: Escherichia coli BL21(DE3)