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PDBsum entry 3ezz

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protein ligands Protein-protein interface(s) links
Hydrolase PDB id
3ezz
Jmol
Contents
Protein chains
(+ 0 more) 144 a.a. *
Ligands
SO4 ×9
* Residue conservation analysis
PDB id:
3ezz
Name: Hydrolase
Title: Crystal structure of human mkp-2
Structure: Dual specificity protein phosphatase 4. Chain: a, b, c, d, e, f. Fragment: catalytic domain. Synonym: mitogen-activated protein kinase phosphatase 2, map kinase phosphatase 2, mkp-2, dual specificity protein phosphatase hvh2. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: dusp4, mkp2, vh2. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.90Å     R-factor:   0.219     R-free:   0.242
Authors: D.G.Jeong,S.K.Jung,S.E.Ryu,S.J.Kim
Key ref:
D.G.Jeong et al. (2009). Crystal structure of the catalytic domain of human MKP-2 reveals a 24-mer assembly. Proteins, 76, 763-767. PubMed id: 19415758 DOI: 10.1002/prot.22423
Date:
24-Oct-08     Release date:   25-Aug-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q13115  (DUS4_HUMAN) -  Dual specificity protein phosphatase 4
Seq:
Struc:
394 a.a.
144 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class 1: E.C.3.1.3.16  - 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
+ 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     3 terms  

 

 
    reference    
 
 
DOI no: 10.1002/prot.22423 Proteins 76:763-767 (2009)
PubMed id: 19415758  
 
 
Crystal structure of the catalytic domain of human MKP-2 reveals a 24-mer assembly.
D.G.Jeong, S.K.Jung, T.S.Yoon, E.J.Woo, J.H.Kim, B.C.Park, S.E.Ryu, S.J.Kim.
 
  ABSTRACT  
 
No abstract given.

 
  Selected figure(s)  
 
Figure 1.
Figure 1. (a) A ribbon diagram of the Cys^280-Ser mutant of the MKP-2C protomer. Secondary structural elements are labeled. The bound sulfate ion indicates the position of the phosphate moiety of the substrate, (b) C trace of MKP-2C is superimposed with that of VHR21 (pdb code: 1VHR). GA: general acid residue (Asp 249 in MKP-2C), (c) Ribbon diagram of 24-mer MKP-2C viewed along the pseudo-octahedral axis of symmetry. Each protomer belonging to an individual tetrameric unit is represented in the same color (cyan, yellow, green, blue, orange and magenta). Fourfold NCS axes and the positions of catalytic C280S are indicated, (d) Surface model of MKP-2C. The surfaces of the MKP-2C 24-mer are shown. The point of view and the color scheme are the same as in Figure 1(c). A tetramer located at the top is omitted to allow a clear view of the hollow space in the interior region, and (e) A stereo diagram of the superimposed crystal structures of MKP-2C (pdb code: 3EZZ; black), MKP-5C (pdb code: 1ZZW; green) and MKP-3C (pdb code: 1MKP; red). The structures were superimposed using the program O.[18] The catalytic C280S is indicated as a black sphere.
 
  The above figure is reprinted by permission from John Wiley & Sons, Inc.: Proteins (2009, 76, 763-767) copyright 2009.