PDBsum entry 2nt2

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Hydrolase PDB id
Jmol PyMol
Protein chains
142 a.a. *
SO4 ×3
Waters ×91
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Crystal structure of slingshot phosphatase 2
Structure: Protein phosphatase slingshot homolog 2. Chain: a, b, c. Fragment: catalytic domain, residues 305-449. Synonym: slingshot phosphatase 2, ssh-2l, hssh-2l. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ssh2, kiaa1725, ssh2l. Expressed in: escherichia coli. Expression_system_taxid: 562.
2.10Å     R-factor:   0.144     R-free:   0.174
Authors: S.K.Jung,D.G.Jeong,T.S.Yoon,J.H.Kim,S.E.Ryu,S.J.Kim
Key ref:
S.K.Jung et al. (2007). Crystal structure of human slingshot phosphatase 2. Proteins, 68, 408-412. PubMed id: 17427953 DOI: 10.1002/prot.21399
06-Nov-06     Release date:   05-Jun-07    
Go to PROCHECK summary

Protein chains
-  (POLG_HAVHM) - 
Protein chains
Pfam   ArchSchema ?
Q76I76  (SSH2_HUMAN) -  Protein phosphatase Slingshot homolog 2
1423 a.a.
142 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class 1: 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
+ phosphate
   Enzyme class 2: 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
+ 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!
  Cellular component     cytoskeleton   1 term 
  Biological process     dephosphorylation   2 terms 
  Biochemical function     phosphatase activity     2 terms  


DOI no: 10.1002/prot.21399 Proteins 68:408-412 (2007)
PubMed id: 17427953  
Crystal structure of human slingshot phosphatase 2.
S.K.Jung, D.G.Jeong, T.S.Yoon, J.H.Kim, S.E.Ryu, S.J.Kim.
No abstract given.

  Selected figure(s)  
Figure 1.
Figure 1. (a) A ribbon diagram of the SSH2-C. Secondary structural elements (helix, orange; strand, blue; loop, grey), which were assigned with the program PROCHECK,[16] are labeled. Catalytic triads (D377, C392S, and R398) and bound sulfate ion are shown as a ball-and-stick representation. Boundaries of secondary structural elements are 1 (309-312), 2(315-318), 3(334-339), 4(353-356), 5(387-391), 1(320-323), 2(326-331), 3(371-383), 4(398-411), 5(415-425), and 6(433-447). (b) The superpositions of seven DSP structures representing each subfamily. A C trace of the DSP18 is superposed with that of VHR. Worm model is in blue for SSH2-C, orange for MKP-3 (pdb code:1mkp), green for VHR (pdb code:1vhr), cyan for PRL-1 (pdb code:1xm2), yellow for CDC14B (pdb code:1ohe), red for PTEN (pdb code:1d5r), and magenta for myotubularin2 (pdb code:1m7r), respectively. The superposition statistics against SSH2-C is 1.5/142 for MKP-3, 1.3/143 for VHR, 1.7/121 for PRL-1, 1.6/121 for CDC14B, 1.6/124 for PTEN, and 2.2/113 for Myotubularin2 where the former value refers to rms deviations and that the latter one refers to the number of superposed C atoms. The position of catalytic cysteine is indicated as a grey ball. (c) C trace of SSH2-C is superimposed with that of the VHR. The region cannot be aligned are colored green, whereas those of SSH2-C are missing are colored red. The point of view is the same as Figure 1(a). (d) The sliced view of active sites for SSH2-C and VHR. The molecular surface diagrams, which were produced using the program VOIDOO,[20] are drawn as a basket-weaved model. It shows the depth and width of the active site pocket for SSH-2C and VHR. The positions of catalytic cysteines are labeled in the figure.
  The above figure is reprinted by permission from John Wiley & Sons, Inc.: Proteins (2007, 68, 408-412) copyright 2007.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19770498 G.T.Lountos, J.E.Tropea, S.Cherry, and D.S.Waugh (2009).
Overproduction, purification and structure determination of human dual-specificity phosphatase 14.
  Acta Crystallogr D Biol Crystallogr, 65, 1013-1020.
PDB code: 2wgp
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