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protein links
Hydrolase PDB id
2e0t
Jmol
Contents
Protein chain
150 a.a. *
Waters ×263
* Residue conservation analysis
PDB id:
2e0t
Name: Hydrolase
Title: Crystal structure of catalytic domain of dual specificity ph 26, ms0830 from homo sapiens
Structure: Dual specificity phosphatase 26. Chain: a. Fragment: catalytic domain, residues 61-211. Synonym: ms0830, putative, low-molecular-mass dual- specifi phosphatase 4, dual-specificity phosphatase skrp3, mitogen- protein kinase phosphatase 8, nata1 protein, cdna flj31142 imr322001317, weakly similar to homo sapiens protein phosph engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Other_details: cell-free protein synthesis
Resolution:
1.67Å     R-factor:   0.172     R-free:   0.212
Authors: Y.Xie,S.Kishishita,K.Murayama,C.Hori-Takemoto,L.Chen,Z.J.Liu B.C.Wang,M.Shirozu,S.Yokoyama,Riken Structural Genomics/pro Initiative (Rsgi)
Key ref: Y.Xie et al. Crystal structure of catalytic domain of dual specificity phosphatase 26, Ms0830 from homo sapiens. To be published,
Date:
13-Oct-06     Release date:   16-Oct-07    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9BV47  (DUS26_HUMAN) -  Dual specificity protein phosphatase 26
Seq:
Struc:
211 a.a.
150 a.a.
Key:    PfamA domain  Secondary structure

 Enzyme reactions 
   Enzyme class 2: E.C.3.1.3.16  - Phosphoprotein phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: A phosphoprotein + H2O = a protein + phosphate
phosphoprotein
+ H(2)O
= protein
+ phosphate
   Enzyme class 3: E.C.3.1.3.48  - Protein-tyrosine-phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Protein tyrosine phosphate + H2O = protein tyrosine + phosphate
Protein tyrosine phosphate
+ H(2)O
= protein tyrosine
+ phosphate
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     dephosphorylation   2 terms 
  Biochemical function     phosphatase activity     3 terms