› 2pk0

X-ray diffraction
2.65Å resolution

Structure of the S. agalactiae serine/threonine phosphatase at 2.65 resolution

Released:
DOI: 10.2210/pdb2pk0/pdb
Model geometry
Fit model/data
PDB entry 2pk0 coloured by chain, front view.
PDB entry 2pk0 coloured by chain, side view.
PDB entry 2pk0 coloured by chain, top view.
Source organism: Streptococcus agalactiae A909
Primary publication:
Structure of Streptococcus agalactiae serine/threonine phosphatase. The subdomain conformation is coupled to the binding of a third metal ion.
Rantanen MK, Lehtiö L, Rajagopal L, Rubens CE, Goldman A
FEBS J 274 3128-37 (2007)
PMID: 17521332

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-186610 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
protein-serine/threonine phosphatase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 250 amino acids
Theoretical weight: 27.4 KDa
Source organism: Streptococcus agalactiae A909
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8VQA1 (Residues: 1-245; Coverage: 100%)
Gene names: AX245_06530, C4618_07995, C6N13_02665, NCTC8184_02176, NCTC9828_02264, WA45_00275, stp1
Sequence domains: Protein phosphatase 2C
Structure domains: PPM-type phosphatase domain

Ligands and Environments

3 bound ligands:
Ligand MG 10 x MG
Ligand GOL 1 x GOL
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21212
Unit cell:
a: 139.4Å b: 92.1Å c: 86.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.197 0.271
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

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

9 mentions without citation

Regulation of transcription by eukaryotic-like serine-threonine kinases and phosphatases in Gram-positive bacterial pathogens.
Wright et al. (2014)
8 more