2img

X-ray diffraction
1.93Å resolution

Crystal structure of dual specificity protein phosphatase 23 from Homo sapiens in complex with ligand malate ion

Released:

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:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-189762 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity protein phosphatase 23 Chain: A
Molecule details ›
Chain: A
Length: 151 amino acids
Theoretical weight: 16.73 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9BVJ7 (Residues: 2-150; Coverage: 99%)
Gene names: DUSP23, LDP3, VHZ
Sequence domains: Dual specificity phosphatase, catalytic domain
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P212121
Unit cell:
a: 35.97Å b: 59.253Å c: 64.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.195 0.229
Expression system: Escherichia coli