› 3qy7

X-ray diffraction
1.62Å resolution

Crystal structures of YwqE from Bacillus subtilis and CpsB from Streptococcus pneumoniae, unique metal-dependent tyrosine phosphatases

Released:
DOI: 10.2210/pdb3qy7/pdb
PDB entry 3qy7 coloured by chain, front view.
PDB entry 3qy7 coloured by chain, side view.
PDB entry 3qy7 coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
Crystal structures of YwqE from Bacillus subtilis and CpsB from Streptococcus pneumoniae, unique metal-dependent tyrosine phosphatases.
Kim HS, Lee SJ, Yoon HJ, An DR, Kim DJ, Kim SJ, Suh SW
J Struct Biol 175 442-50 (2011)
PMID: 21605684

Function and Biology Details

Reaction catalysed: 
Protein tyrosine phosphate + H(2)O = protein tyrosine + 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-161245 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein phosphatase YwqE Chain: A
Molecule details ›
Chain: A
Length: 262 amino acids
Theoretical weight: 30.07 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P96717 (Residues: 1-254; Coverage: 100%)
Gene names: BSU36240, ywqE
Sequence domains: Capsular polysaccharide synthesis, CpsB/CapC
Structure domains: Metal-dependent hydrolases

Ligands and Environments

3 bound ligands:
Ligand FE 2 x FE
Ligand MG 1 x MG
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 4A
Spacegroup: P212121
Unit cell:
a: 36.449Å b: 47.311Å c: 132.013Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.207 0.247
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Protein tyrosine phosphatase structure-function relationships in regulation and pathogenesis.
Böhmer et al. (2013)
3 more

1 mention without citation

Porphyromonas gingivalis Tyrosine Phosphatase Php1 Promotes Community Development and Pathogenicity.
Jung et al. (2019)