PDBsum entry 1c0e

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protein ligands Protein-protein interface(s) links
Hydrolase PDB id
Protein chains
154 a.a. *
PO4 ×2
Waters ×98
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Active site s19a mutant of bovine heart phosphotyrosyl phosphatase
Structure: Protein (tyrosine phosphatase (orthophosphoric monoester phosphohydrolase)). Chain: a, b. Engineered: yes. Mutation: yes
Source: Bos taurus. Cattle. Organism_taxid: 9913. Organ: heart. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit: Dimer (from PQS)
2.20Å     R-factor:   0.191     R-free:   0.244
Authors: L.Tabernero,B.N.Evans,P.A.Tishmack,R.L.Van Etten, C.V.Stauffacher
Key ref:
L.Tabernero et al. (1999). The structure of the bovine protein tyrosine phosphatase dimer reveals a potential self-regulation mechanism. Biochemistry, 38, 11651-11658. PubMed id: 10512620 DOI: 10.1021/bi990381x
15-Jul-99     Release date:   28-Sep-99    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P11064  (PPAC_BOVIN) -  Low molecular weight phosphotyrosine protein phosphatase
158 a.a.
154 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class 2: E.C.  - Acid phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: A phosphate monoester + H2O = an alcohol + phosphate
phosphate monoester
+ H(2)O
= alcohol
Bound ligand (Het Group name = PO4)
corresponds exactly
   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
Bound ligand (Het Group name = PO4)
corresponds exactly
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   1 term 
  Biological process     peptidyl-tyrosine dephosphorylation   2 terms 
  Biochemical function     hydrolase activity     5 terms  


DOI no: 10.1021/bi990381x Biochemistry 38:11651-11658 (1999)
PubMed id: 10512620  
The structure of the bovine protein tyrosine phosphatase dimer reveals a potential self-regulation mechanism.
L.Tabernero, B.N.Evans, P.A.Tishmack, R.L.Van Etten, C.V.Stauffacher.
The bovine protein tyrosine phosphatase (BPTP) is a member of the class of low-molecular weight protein tyrosine phosphatases (PTPases) found to be ubiquitous in mammalian cells. The catalytic site of BPTP contains a CX(5)R(S/T) phosphate-binding motif or P-loop (residues 12-19) which is the signature sequence for all PTPases. Ser19, the final residue of the P-loop motif, interacts with the catalytic Cys12 and participates in stabilizing the conformation of the active site through interactions with Asn15, also in the P-loop. Mutations at Ser19 result in an enzyme with altered kinetic properties with changes in the pK(a) of the neighboring His72. The X-ray structure of the S19A mutant enzyme shows that the general conformation of the P-loop is preserved. However, changes in the loop containing His72 result in a displacement of the His72 side chain that may explain the shift in the pK(a). In addition, it was found that in the crystal, the protein forms a dimer in which Tyr131 and Tyr132 from one monomer insert into the active site of the other monomer, suggesting a dual-tyrosine motif on target sites for this enzyme. Since the activity of this PTPase is reportedly regulated by phosphorylation at Tyr131 and Tyr132, the structure of this dimer may provide a model of a self-regulation mechanism for the low-molecular weight PTPases.

Literature references that cite this PDB file's key reference

  PubMed id Reference
19678837 J.Blobel, P.Bernadó, H.Xu, C.Jin, and M.Pons (2009).
Weak oligomerization of low-molecular-weight protein tyrosine phosphatase is conserved from mammals to bacteria.
  FEBS J, 276, 4346-4357.  
18298793 L.Tabernero, A.R.Aricescu, E.Y.Jones, and S.E.Szedlacsek (2008).
Protein tyrosine phosphatases: structure-function relationships.
  FEBS J, 275, 867-882.  
16253994 A.P.Zabell, A.D.Schroff, B.E.Bain, R.L.Van Etten, O.Wiest, and C.V.Stauffacher (2006).
Crystal structure of the human B-form low molecular weight phosphotyrosyl phosphatase at 1.6-A resolution.
  J Biol Chem, 281, 6520-6527.
PDB code: 1xww
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