PDBsum entry 2wgp

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protein ligands Protein-protein interface(s) links
Hydrolase PDB id
Protein chain
168 a.a. *
PO4 ×2
Waters ×347
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Crystal structure of human dual specificity phosphatase 14
Structure: Dual specificity protein phosphatase 14. Chain: a, b. Fragment: residues 2-191. Synonym: dual specificity phosphatase 14, mitogen-activated kinase phosphatase 6, mkp-1-like protein tyrosine phosphat kinase phosphatase 6, mkp-6, mkp-l. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.
1.88Å     R-factor:   0.177     R-free:   0.220
Authors: G.T.Lountos,J.E.Tropea,S.Cherry,D.S.Waugh
Key ref:
G.T.Lountos et al. (2009). Overproduction, purification and structure determination of human dual-specificity phosphatase 14. Acta Crystallogr D Biol Crystallogr, 65, 1013-1020. PubMed id: 19770498 DOI: 10.1107/S0907444909023762
22-Apr-09     Release date:   06-Oct-09    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
O95147  (DUS14_HUMAN) -  Dual specificity protein phosphatase 14
198 a.a.
168 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class 2: E.C.  - Protein-serine/threonine phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: [a protein]-serine/threonine phosphate + H2O = [a protein]- serine/threonine + phosphate
[a protein]-serine/threonine phosphate
+ H(2)O
= [a protein]- serine/threonine
Bound ligand (Het Group name = PO4)
corresponds exactly
   Enzyme class 3: E.C.  - Protein-tyrosine-phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Protein tyrosine phosphate + H2O = protein tyrosine + phosphate
Protein tyrosine phosphate
+ H(2)O
= protein tyrosine
Bound ligand (Het Group name = PO4)
corresponds exactly
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     peptidyl-tyrosine dephosphorylation   4 terms 
  Biochemical function     hydrolase activity     7 terms  


DOI no: 10.1107/S0907444909023762 Acta Crystallogr D Biol Crystallogr 65:1013-1020 (2009)
PubMed id: 19770498  
Overproduction, purification and structure determination of human dual-specificity phosphatase 14.
G.T.Lountos, J.E.Tropea, S.Cherry, D.S.Waugh.
Dual-specificity phosphatases (DUSPs) are enzymes that participate in the regulation of biological processes such as cell growth, differentiation, transcription and metabolism. A number of DUSPs are able to dephosphorylate phosphorylated serine, threonine and tyrosine residues on mitogen-activated protein kinases (MAPKs) and thus are also classified as MAPK phosphatases (MKPs). As an increasing number of DUSPs are being identified and characterized, there is a growing need to understand their biological activities at the molecular level. There is also significant interest in identifying DUSPs that could be potential targets for drugs that modulate MAPK-dependent signaling and immune responses, which have been implicated in a variety of maladies including cancer, infectious diseases and inflammatory disorders. Here, the overproduction, purification and crystal structure at 1.88 A resolution of human dual-specificity phosphatase 14, DUSP14 (MKP6), are reported. This structural information should accelerate the study of DUSP14 at the molecular level and may also accelerate the discovery and development of novel therapeutic agents.
  Selected figure(s)  
Figure 2.
Figure 2 Ribbon representation of the three-dimensional structure of monomeric DUSP14.
Figure 6.
Figure 6 Stereoview of the superimposed coordinates of DUSP14 (PDB code 2wgp ; cyan) and DUSP18 (PDB code 2esb ; red).
  The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2009, 65, 1013-1020) copyright 2009.  
  Figures were selected by an automated process.