2vsw

X-ray diffraction
2.2Å resolution

The structure of the rhodanese domain of the human dual specificity phosphatase 16

Released:
Source organism: Homo sapiens
Entry authors: Murray JW, Barr A, Pike ACW, Elkins J, Phillips C, Wang J, Savitsky P, Roos A, Bishop S, Wickstroem M, Bountra C, Edwards AM, Arrowsmith CH, Burgess-Brown N, Pantic N, Bray J, von Delft F, Gileadi O, Knapp S

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
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-189823 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity protein phosphatase 16 Chains: A, B
Molecule details ›
Chains: A, B
Length: 153 amino acids
Theoretical weight: 17.07 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9BY84 (Residues: 5-150; Coverage: 22%)
Gene names: DUSP16, KIAA1700, MKP7
Sequence domains: Rhodanese-like domain
Structure domains: Rhodanese-like domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P21212
Unit cell:
a: 70.451Å b: 69.128Å c: 61.017Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.169 0.227
Expression system: Escherichia coli BL21(DE3)