PDBsum entry: 2nt2

Hydrolase

PDB id: 2nt2

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

Protein chains

Q76I76  (SSH2_HUMAN) -  Protein phosphatase Slingshot homolog 2

Seq: 1423 a.a.

Struc: 142 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class 1: E.C.3.1.3.16 - Phosphoprotein phosphatase.
• Reaction: A phosphoprotein + H₂O = a protein + phosphate
• Enzyme class 2: E.C.3.1.3.48 - Protein-tyrosine-phosphatase.
• Reaction: Protein tyrosine phosphate + H₂O = 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 

• 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.