› 2gwo

X-ray diffraction
2.4Å resolution

crystal structure of TMDP

Released:
DOI: 10.2210/pdb2gwo/pdb
PDB entry 2gwo coloured by chain, front view.
PDB entry 2gwo coloured by chain, side view.
PDB entry 2gwo coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of human TMDP, a testis-specific dual specificity protein phosphatase: implications for substrate specificity.
Kim SJ, Jeong DG, Yoon TS, Son JH, Cho SK, Ryu SE, Kim JH
Proteins 66 239-45 (2007)
PMID: 17044055

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193789 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity protein phosphatase 13B 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, SKRP4, 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

Quick links

Citations

1 review citation

Structure and catalytic mechanism of human protein tyrosine phosphatome.
Kim et al. (2012)
7 other articles

2 mentions without citation

Structural Insight into the Critical Role of the N-Terminal Region in the Catalytic Activity of Dual-Specificity Phosphatase 26.
Won et al. (2016)
1 more