› 1vhr

X-ray diffraction
2.1Å resolution

HUMAN VH1-RELATED DUAL-SPECIFICITY PHOSPHATASE

Released:
DOI: 10.2210/pdb1vhr/pdb
PDB entry 1vhr coloured by chain, front view.
PDB entry 1vhr coloured by chain, side view.
PDB entry 1vhr coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of the dual specificity protein phosphatase VHR.
Yuvaniyama J, Denu JM, Dixon JE, Saper MA
Science 272 1328-31 (1996)
PMID: 8650541

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:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156340 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity protein phosphatase 3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 184 amino acids
Theoretical weight: 20.37 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P51452 (Residues: 2-185; Coverage: 100%)
Gene names: DUSP3, VHR
Sequence domains: Dual specificity phosphatase, catalytic domain
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

2 bound ligands:
Ligand EPE 1 x EPE
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 61.148Å b: 60.04Å c: 52.016Å
α: 90° β: 98.35° γ: 90°
R-values:
R R work R free
0.176 0.176 0.254
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

44 review citations

Protein tyrosine phosphatases in the human genome.
Alonso et al. (2004)
43 more

21 mentions without citation

Structural biology of glucan phosphatases from humans to plants.
Gentry et al. (2016)
20 more