3tg3

X-ray diffraction
2.68Å resolution

Crystal structure of the MAPK binding domain of MKP7

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
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
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, C, D
Molecule details ›
Chains: A, B, C, D
Length: 142 amino acids
Theoretical weight: 15.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9BY84 (Residues: 5-138; Coverage: 20%)
Gene names: DUSP16, KIAA1700, MKP7
Sequence domains: Rhodanese-like domain
Structure domains: Rhodanese-like domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P1
Unit cell:
a: 40.497Å b: 47.479Å c: 64.512Å
α: 91.18° β: 97.29° γ: 96.81°
R-values:
R R work R free
0.278 0.239 0.288
Expression system: Escherichia coli