PDBe 2gwo

X-ray diffraction
2.4Å resolution

crystal structure of TMDP

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. 
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity protein phosphatase 13 isoform B Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 198 amino acids
Theoretical weight: 22.17 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UII6 (Residues: 1-198; Coverage: 100%)
Gene names: DUSP13, DUSP13B, TMDP
Sequence domains: Dual specificity phosphatase, catalytic domain
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-18B
Spacegroup: P21
Unit cell:
a: 61.586Å b: 72.24Å c: 89.896Å
α: 90° β: 99.66° γ: 90°
R-values:
R R work R free
0.198 0.198 0.25
Expression system: Escherichia coli