PDBsum entry 4erc

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Hydrolase PDB id
Protein chains
150 a.a.
VN4 ×2
Waters ×439
PDB id:
Name: Hydrolase
Title: Structure of vhz bound to metavanadate
Structure: Dual specificity protein phosphatase 23. Chain: a, b. Synonym: low molecular mass dual specificity phosphatase 3, vh1-like phosphatase z. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: dusp23, ldp3, vhz. Expressed in: escherichia coli. Expression_system_taxid: 511693.
1.15Å     R-factor:   0.129     R-free:   0.145
Authors: K.Vyacheslav,C.H.Alvan,J.J.Sean
Key ref: V.I.Kuznetsov et al. (2012). New aspects of the phosphatase VHZ revealed by a high-resolution structure with vanadate and substrate screening. Biochemistry, 51, 9869-9879. PubMed id: 23145819 DOI: 10.1021/bi300908y
19-Apr-12     Release date:   19-Dec-12    
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Protein chains
Pfam   ArchSchema ?
Q9BVJ7  (DUS23_HUMAN) -  Dual specificity protein phosphatase 23
150 a.a.
150 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class 2: 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 3: 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     cytoplasm   4 terms 
  Biological process     peptidyl-tyrosine dephosphorylation   3 terms 
  Biochemical function     hydrolase activity     5 terms  


DOI no: 10.1021/bi300908y Biochemistry 51:9869-9879 (2012)
PubMed id: 23145819  
New aspects of the phosphatase VHZ revealed by a high-resolution structure with vanadate and substrate screening.
V.I.Kuznetsov, A.C.Hengge, S.J.Johnson.
The recently discovered 150-residue human VHZ (VH1-related protein, Z member) is one of the smallest protein tyrosine phosphatases (PTPs) known and contains only the minimal structural elements common to all PTPs. We report a substrate screening analysis and a crystal structure of the VHZ complex with vanadate at 1.1 Å resolution, with a detailed structural comparison with other members of the protein tyrosine phosphatase family, including classical tyrosine-specific protein tyrosine phosphatases (PTPs) and dual-specificity phosphatases (DSPs). A screen with 360 phosphorylated peptides shows VHZ efficiently catalyzes the hydrolysis of phosphotyrosine (pY)-containing peptides but exhibits no activity toward phosphoserine (pS) or phosphothreonine (pT) peptides. The new structure reveals a deep and narrow active site more typical of the classical tyrosine-specific PTPs. Despite the high degrees of structural and sequence similarity between VHZ and classical PTPs, its general acid IPD-loop is most likely conformationally rigid, in contrast to the flexible WPD counterpart of classical PTPs. VHZ also lacks substrate recognition domains and other domains typically found on classical PTPs. It is therefore proposed that VHZ is more properly classified as an atypical PTP rather than an atypical DSP, as has been suggested.