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PDBsum entry 2nt2

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protein ligands Protein-protein interface(s) links
Hydrolase PDB id
2nt2
Jmol PyMol
Contents
Protein chains
142 a.a. *
Ligands
SO4 ×3
Waters ×91
* Residue conservation analysis
PDB id:
2nt2
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.
Resolution:
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
Date:
06-Nov-06     Release date:   05-Jun-07    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam  
-  (POLG_HAVHM) - 
Protein chains
Pfam   ArchSchema ?
Q76I76  (SSH2_HUMAN) -  Protein phosphatase Slingshot homolog 2
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
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.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!
  Cellular component     cytoskeleton   1 term 
  Biological process     dephosphorylation   2 terms 
  Biochemical function     phosphatase activity     2 terms  

 

 
    reference    
 
 
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.
 
  ABSTRACT  
 
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
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 code is shown on the right.

 

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