› 2jfr

X-ray diffraction
0.83Å resolution

Crystal structure of the PPM Ser-Thr phosphatase MsPP from Mycobacterium smegmatis in complex with phosphate at 0.83 A resolution

Released:
DOI: 10.2210/pdb2jfr/pdb
PDB entry 2jfr coloured by chain, front view.
PDB entry 2jfr coloured by chain, side view.
PDB entry 2jfr coloured by chain, top view.
Source organism: Mycolicibacterium smegmatis MC2 155
Primary publication:
Insights into the catalytic mechanism of PPM Ser/Thr phosphatases from the atomic resolution structures of a mycobacterial enzyme.
Bellinzoni M, Wehenkel A, Shepard W, Alzari PM
Structure 15 863-72 (2007)
PMID: 17637345

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:
  • not assigned
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 MC2 155
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

4 bound ligands:
Ligand MG 4 x MG
Ligand MN 1 x MN
Ligand CL 1 x CL
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7A
Spacegroup: P21212
Unit cell:
a: 76.382Å b: 83.998Å c: 33.478Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.096 not available 0.124
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

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

5 mentions without citation

Development of a new physics-based internal coordinate mechanics force field and its application to protein loop modeling.
Arnautova et al. (2011)
4 more