› 3d6a

X-ray diffraction
2.25Å resolution

Crystal structure of the 2H-phosphatase domain of Sts-2 in complex with tungstate.

Released:
DOI: 10.2210/pdb3d6a/pdb
PDB entry 3d6a coloured by chain, front view.
PDB entry 3d6a coloured by chain, side view.
PDB entry 3d6a coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Structural and functional characterization of the 2H-phosphatase domain of Sts-2 reveals an acid-dependent phosphatase activity.
Chen Y, Jakoncic J, Carpino N, Nassar N
Biochemistry 48 1681-90 (2009)
PMID: 19196006

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-174868 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin-associated and SH3 domain-containing protein A Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 273 amino acids
Theoretical weight: 30.72 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q3V3E1 (Residues: 354-622; Coverage: 43%)
Gene names: Sts2, Ubash3a
Sequence domains: Histidine phosphatase superfamily (branch 1)
Structure domains: Phosphoglycerate mutase-like

Ligands and Environments

3 bound ligands:
Ligand MG 9 x MG
Ligand NA 4 x NA
Ligand W 4 x W
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X6A
Spacegroup: P212121
Unit cell:
a: 78.205Å b: 116.665Å c: 121.471Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.208 0.257
Expression system: Escherichia coli

Quick links

Citations

6 review citations

The extended human PTPome: a growing tyrosine phosphatase family.
Alonso et al. (2016)
5 more

1 mention without citation

Structural and functional characterization of the 2H-phosphatase domain of Sts-2 reveals an acid-dependent phosphatase activity.
Chen et al. (2009)