› 2v06

X-ray diffraction
1.05Å resolution

Crystal structure of the PPM Ser-Thr phosphatase MsPP from Mycobacterium smegmatis at pH 5.5

Released:
DOI: 10.2210/pdb2v06/pdb
PDB entry 2v06 coloured by chain, front view.
PDB entry 2v06 coloured by chain, side view.
PDB entry 2v06 coloured by chain, top view.
Source organism: Mycolicibacterium smegmatis
Primary publication:
Structural and binding studies of the three-metal center in two mycobacterial PPM Ser/Thr protein phosphatases.
Wehenkel A, Bellinzoni M, Schaeffer F, Villarino A, Alzari PM
J Mol Biol 374 890-8 (2007)
PMID: 17961594

Function and Biology Details

Reaction catalysed: 
[a protein]-serine/threonine phosphate + H(2)O = [a protein]-serine/threonine + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-106315 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
protein-serine/threonine phosphatase Chain: A
Molecule details ›
Chain: A
Length: 234 amino acids
Theoretical weight: 24.28 KDa
Source organism: Mycolicibacterium smegmatis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0QTQ6 (Residues: 1-233; Coverage: 100%)
Gene name: MSMEG_1928
Sequence domains: Protein phosphatase 2C
Structure domains: PPM-type phosphatase domain

Ligands and Environments

2 bound ligands:
Ligand MG 3 x MG
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: P21212
Unit cell:
a: 74.718Å b: 83.596Å c: 33.638Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.133 not available 0.188
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 review citations

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

2 mentions without citation

Preclinical pharmacology, antitumor activity, and development of pharmacodynamic markers for the novel, potent AKT inhibitor CCT128930.
Yap et al. (2011)
1 more