› 7moe

X-ray diffraction
1.7Å resolution

Crystal Structure of Arabidopsis thaliana Plant and Fungi Atypical Dual Specificity Phosphatase 1(AtPFA-DSP1)Cys150Ser in complex with 5-diphosphoinositol 1,2,3,4,6-pentakisphosphate (5-InsP7)

Released:
DOI: 10.2210/pdb7moe/pdb
Model geometry
Fit model/data
PDB entry 7moe coloured by chain, front view.
PDB entry 7moe coloured by chain, side view.
PDB entry 7moe coloured by chain, top view.
Source organism: Arabidopsis thaliana
Primary publication:
A structural exposé of noncanonical molecular reactivity within the protein tyrosine phosphatase WPD loop.
Wang H, Perera L, Jork N, Zong G, Riley AM, Potter BVL, Jessen HJ, Shears SB
OpenAccess logo Nat Commun 13 2231 (2022)
PMID: 35468885

Function and Biology Details

Reaction catalysed: 
Diphospho-myo-inositol polyphosphate + H(2)O = myo-inositol polyphosphate + 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-195719 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Inositol diphosphatase DSP1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 171 amino acids
Theoretical weight: 19.64 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9ZVN4 (Residues: 49-215; Coverage: 78%)
Gene names: At1g05000, DSP1, PTP135, T7A14.14
Sequence domains: Tyrosine phosphatase family

Ligands and Environments

1 bound ligand:
Ligand I7P 2 x I7P
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P213
Unit cell:
a: 124.602Å b: 124.602Å c: 124.602Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.122 0.12 0.149
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Loop dynamics and the evolution of enzyme activity.
Corbella et al. (2023)
1 more

1 mention without citation

A structural exposé of noncanonical molecular reactivity within the protein tyrosine phosphatase WPD loop.
Wang et al. (2022)