PDBsum entry: 2g6z

Hydrolase

PDB id: 2g6z

Contents

Protein chains

147 a.a. *

Ligands

SO4 ×6

Waters ×39

* Residue conservation analysis

PDB id:

2g6z

Name:

Hydrolase

Title:

Crystal structure of human dusp5

Structure:

Dual specificity protein phosphatase 5. Chain: a, b, c. Fragment: residues 174-384. Synonym: dusp5, dual specificity protein phosphatase hvh3, tyrosine-protein phosphatase. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

2.70Å R-factor: 0.244 R-free: 0.291

Authors:

S.J.Kim,S.E.Ryu

Key ref:

D.G.Jeong et al. (2007). Crystal structure of the catalytic domain of human DUSP5, a dual specificity MAP kinase protein phosphatase. Proteins, 66, 253-258. PubMed id: 17078075 DOI: 10.1002/prot.21224

Date:

26-Feb-06 Release date: 16-Jan-07

Protein chains

Q16690  (DUS5_HUMAN) -  Dual specificity protein phosphatase 5

Seq: 384 a.a.

Struc: 147 a.a.*

* PDB and UniProt seqs differ at 6 residue positions (black crosses)

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 (3 terms)

reference

DOI no: 10.1002/prot.21224

Proteins 66:253-258 (2007)

PubMed id: 17078075

Crystal structure of the catalytic domain of human DUSP5, a dual specificity MAP kinase protein phosphatase.

D.G.Jeong, Y.H.Cho, T.S.Yoon, J.H.Kim, S.E.Ryu, S.J.Kim.

ABSTRACT

No abstract given.

Selected figure(s)

Figure 1.
Figure 1. (a) C trace of the DUSP5-C structure (black) superimposed with that of VHR (red; pdb code, 1VHR). The regions of DUSP5-C that cannot be aligned are shown in green. The secondary structural elements of DUSP5-C are labeled black whereas the secondary structural elements unique to VHR are labeled red. GA indicates the position of the general acid loop. (b) The active site of DUSP5-C. The active site of DUSP5-C (ivory) is superimposed with that of MKP3 (grey). C263S-R269, D232, and bound sulfate ion are shown for DUSP5-C, whereas C293-R299 and D262 are shown for MKP3. The hydrogen bonding interactions for DUSP5-C are indicated with dotted lines. The residues of DUSP5-C are shown in black whereas those for MKP are labeled red. Some side-chains were omitted from the drawing for clarity. (c) C trace of the DUSP5-C structure (black) is superimposed with that of the MKP-3 structure (red; pdb code, 1MKP). The regions of DUSP5-C that cannot be aligned are shown in green. The secondary structural elements for DUSP5-C are shown in black, whereas the secondary structural elements unique to MKP-3 are shown in red. (d) Ribbon diagram of a DUSP5-C dimer. Protomers A and B are shown in magenta and grey, respectively. Catalytically active residues, C263(A) and C263(B) and bound sulfate ions are represented with ball-and-stick models. (e) Stereodiagram of the 2Fo-Fc electron density map around the active site superposed on the refined model. The map is contoured at 1.2 level. The residues are represented as a ball-and-stick model.

The above figure is reprinted by permission from John Wiley & Sons, Inc.: Proteins (2007, 66, 253-258) copyright 2007.