› 7c8s

X-ray diffraction
1.31Å resolution

Crystal structure of DUSP22 mutant_N128A

Released:
DOI: 10.2210/pdb7c8s/pdb
PDB entry 7c8s coloured by chain, front view.
PDB entry 7c8s coloured by chain, side view.
PDB entry 7c8s coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural Insights into the Active Site Formation of DUSP22 in N-loop-containing Protein Tyrosine Phosphatases.
Lai CH, Chang CC, Chuang HC, Tan TH, Lyu PC
Int J Mol Sci 21 (2020)
PMID: 33053837

Function and Biology Details

Reactions catalysed: 
[a protein]-serine/threonine phosphate + H(2)O = [a protein]-serine/threonine + phosphate
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate
Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192572 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity protein phosphatase 22 Chain: A
Molecule details ›
Chain: A
Length: 157 amino acids
Theoretical weight: 17.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9NRW4 (Residues: 1-155; Coverage: 84%)
Gene names: DUSP22, JSP1, LMWDSP2, MKPX
Sequence domains: Dual specificity phosphatase, catalytic domain

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL15A1
Spacegroup: C2
Unit cell:
a: 89.842Å b: 50.432Å c: 40.212Å
α: 90° β: 95.96° γ: 90°
R-values:
R R work R free
0.188 0.187 0.196
Expression system: Escherichia coli

Quick links

Citations

2 review citations

A Review of DUSP26: Structure, Regulation and Relevance in Human Disease.
Thompson et al. (2021)
1 more

1 mention without citation

Structural Insights into the Active Site Formation of DUSP22 in N-loop-containing Protein Tyrosine Phosphatases.
Lai et al. (2020)