› 1xri

X-ray diffraction
3.3Å resolution

X-ray structure of a putative phosphoprotein phosphatase from Arabidopsis thaliana gene AT1G05000

Released:
DOI: 10.2210/pdb1xri/pdb
PDB entry 1xri coloured by chain, front view.
PDB entry 1xri coloured by chain, side view.
PDB entry 1xri coloured by chain, top view.
Source organism: Arabidopsis thaliana
Primary publication:
Structural and functional characterization of a novel phosphatase from the Arabidopsis thaliana gene locus At1g05000.
Aceti DJ, Bitto E, Yakunin AF, Proudfoot M, Bingman CA, Frederick RO, Sreenath HK, Vojtik FC, Wrobel RL, Fox BG, Markley JL, Phillips GN
Proteins 73 241-53 (2008)
PMID: 18433060

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 domain:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo hexamer
Assembly name:
PDBe Complex ID:
PDB-CPX-195720 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein phosphatase DSP1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 151 amino acids
Theoretical weight: 17.54 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9ZVN4 (Residues: 52-202; Coverage: 70%)
Gene names: At1g05000, DSP1, PTP135, T7A14.14
Sequence domains: Tyrosine phosphatase family
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

1 bound ligand:
Ligand SO4 4 x SO4
1 modified residue:
Ligand MSE 6 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM, APS BEAMLINE 14-ID-B
Spacegroup: P213
Unit cell:
a: 124.483Å b: 124.483Å c: 124.483Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.204 0.249
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Importance of tyrosine phosphorylation for transmembrane signaling in plants.
Mühlenbeck et al. (2021)
5 other articles

9 mentions without citation

The SeqFEATURE library of 3D functional site models: comparison to existing methods and applications to protein function annotation.
Wu et al. (2008)
8 more