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Hydrolase PDB id
1yz4
Jmol
Contents
Protein chains
159 a.a. *
Ligands
BOG
SO4 ×4
Waters ×94
* Residue conservation analysis
PDB id:
1yz4
Name: Hydrolase
Title: Crystal structure of dusp15
Structure: Dual specificity phosphatase-like 15 isoform a. Chain: a, b. Fragment: catalytic domain. Synonym: dusp15. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Resolution:
2.40Å     R-factor:   0.217     R-free:   0.269
Authors: S.J.Kim,S.E.Ryu,D.G.Jeong,T.S.Yoon,J.H.Kim,Y.H.Cho, S.K.Jeong,J.W.Lee,J.H.Son
Key ref:
T.S.Yoon et al. (2005). Crystal structure of the catalytic domain of human VHY, a dual-specificity protein phosphatase. Proteins, 61, 694-697. PubMed id: 16170801 DOI: 10.1002/prot.20642
Date:
28-Feb-05     Release date:   01-Nov-05    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9H1R2  (DUS15_HUMAN) -  Dual specificity protein phosphatase 15
Seq:
Struc:
295 a.a.
159 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 12 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class 1: 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 2: 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     2 terms  

 

 
    reference    
 
 
DOI no: 10.1002/prot.20642 Proteins 61:694-697 (2005)
PubMed id: 16170801  
 
 
Crystal structure of the catalytic domain of human VHY, a dual-specificity protein phosphatase.
T.S.Yoon, D.G.Jeong, J.H.Kim, Y.H.Cho, J.H.Son, J.W.Lee, S.E.Ryu, S.J.Kim.
 
  ABSTRACT  
 
No abstract given.

 
  Selected figure(s)  
 
Figure 1.
Figure 1. (a) The VHYc structure represented as a ribbon diagram. Secondary structural elements are labeled on the drawing. The bound sulfate ion is represented as a ball-and-stick model. (b) C trace of the VHYc structure (thick line) is superimposed with that of the VHR structure (thin line). The regions of VHYc that cannot be aligned are colored green, whereas the regions of VHYc that are missing are colored red. The point of view is the same as that in (a). (c) Electrostatic potential surfaces of VHYc and VHR are presented. Positive and negative potentials are colored blue and red, respectively. The point of view is the same as that in (a).
 
  The above figure is reprinted by permission from John Wiley & Sons, Inc.: Proteins (2005, 61, 694-697) copyright 2005.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20018849 J.P.Li, Y.N.Fu, Y.R.Chen, and T.H.Tan (2010).
JNK pathway-associated phosphatase dephosphorylates focal adhesion kinase and suppresses cell migration.
  J Biol Chem, 285, 5472-5478.  
17173287 H.M.Chu, and A.H.Wang (2007).
Enzyme-substrate interactions revealed by the crystal structures of the archaeal Sulfolobus PTP-fold phosphatase and its phosphopeptide complexes.
  Proteins, 66, 996.
PDB codes: 2dxp 2i6i 2i6j 2i6m 2i6o 2i6p
17505108 J.Phan, J.E.Tropea, and D.S.Waugh (2007).
Structure-assisted discovery of Variola major H1 phosphatase inhibitors.
  Acta Crystallogr D Biol Crystallogr, 63, 698-704.
PDB code: 2p4d
17427953 S.K.Jung, D.G.Jeong, T.S.Yoon, J.H.Kim, S.E.Ryu, and S.J.Kim (2007).
Crystal structure of human slingshot phosphatase 2.
  Proteins, 68, 408-412.
PDB code: 2nt2
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.