› 5gtj

X-ray diffraction
2Å resolution

CRYSTAL STRUCTURE OF CATALYTICALLY ACTIVE FORM OF HUMAN DUSP26

Released:
DOI: 10.2210/pdb5gtj/pdb
PDB entry 5gtj coloured by chain, front view.
PDB entry 5gtj coloured by chain, side view.
PDB entry 5gtj coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural Insight into the Critical Role of the N-Terminal Region in the Catalytic Activity of Dual-Specificity Phosphatase 26.
Won EY, Lee SO, Lee DH, Lee D, Bae KH, Lee SC, Kim SJ, Chi SW
PLoS One 11 e0162115 (2016)
PMID: 27583453

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189750 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity protein phosphatase 26 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 181 amino acids
Theoretical weight: 20.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9BV47 (Residues: 39-211; Coverage: 82%)
Gene names: DUSP24, DUSP26, LDP4, MKP8, NATA1, SKRP3
Sequence domains: Dual specificity phosphatase, catalytic domain
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

1 bound ligand:
Ligand PO4 4 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 7A (6B, 6C1)
Spacegroup: C2
Unit cell:
a: 122.617Å b: 100.803Å c: 70.87Å
α: 90° β: 114.67° γ: 90°
R-values:
R R work R free
0.199 0.196 0.253
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 citation in other articles

Structural and biochemical analysis of atypically low dephosphorylating activity of human dual-specificity phosphatase 28.
Ku et al. (2017)
2 more

2 mentions without citation

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