› 4d3q

X-ray diffraction
1.64Å resolution

crystal structure of point mutated DUSP19 (R156A)

Released:
DOI: 10.2210/pdb4d3q/pdb
PDB entry 4d3q coloured by chain, front view.
PDB entry 4d3q coloured by chain, side view.
PDB entry 4d3q coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural Analysis of Activity-Modulating Mutations of Dusp19
Jeon TJ, Nam KT, Ryu SE
Biodesign 3 116- (2015)

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186698 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity protein phosphatase 19 Chains: A, B
Molecule details ›
Chains: A, B
Length: 147 amino acids
Theoretical weight: 16.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8WTR2 (Residues: 65-205; Coverage: 65%)
Gene names: DUSP17, DUSP19, LMWDSP3, SKRP1
Sequence domains: Dual specificity phosphatase, catalytic domain
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 7A (6B, 6C1)
Spacegroup: P3121
Unit cell:
a: 86.064Å b: 86.064Å c: 93.539Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.175 0.174 0.196
Expression system: Escherichia coli BL21(DE3)

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