PDBsum entry 2h03

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Hydrolase PDB id
Protein chain
288 a.a. *
_CL ×2
_MG ×2
Waters ×202
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Structural studies of protein tyrosine phosphatase beta cata domain in complex with inhibitors
Structure: Protein tyrosine phosphatase, receptor type, b,. Chain: a. Fragment: catalytic domain, 1676-1970. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ptprb. Expressed in: escherichia coli. Expression_system_taxid: 562.
1.65Å     R-factor:   0.180     R-free:   0.217
Authors: A.G.Evdokimov,M.E.Pokross,R.L.Walter,M.Mekel,J.L.Gray,K.G.Pe M.B.Maier,K.D.Amarasinghe,C.M.Clark,R.Nichols
Key ref: K.K.Amarasinghe et al. (2006). Design and synthesis of potent, non-peptidic inhibitors of HPTPbeta. Bioorg Med Chem Lett, 16, 4252-4256. PubMed id: 16759857 DOI: 10.1016/j.bmcl.2006.05.074
13-May-06     Release date:   13-Jun-06    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P23467  (PTPRB_HUMAN) -  Receptor-type tyrosine-protein phosphatase beta
1997 a.a.
288 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: 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
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     dephosphorylation   2 terms 
  Biochemical function     phosphatase activity     2 terms  


DOI no: 10.1016/j.bmcl.2006.05.074 Bioorg Med Chem Lett 16:4252-4256 (2006)
PubMed id: 16759857  
Design and synthesis of potent, non-peptidic inhibitors of HPTPbeta.
K.K.Amarasinghe, A.G.Evdokimov, A.G.Evidokimov, K.Xu, C.M.Clark, M.B.Maier, A.Srivastava, A.O.Colson, G.S.Gerwe, G.E.Stake, B.W.Howard, M.E.Pokross, J.L.Gray, K.G.Peters.
The sulfamic acid phosphotyrosine mimetic was coupled with a previously known malonate template to obtain highly selective and potent inhibitors of HPTPbeta. Potentially hydrolyzable malonate ester functionalities were replaced with 1,2,4-oxadiazoles without a significant effect on HPTPbeta potency.

Literature references that cite this PDB file's key reference

  PubMed id Reference
19652406 R.A.Neves Filho, C.A.da Silva, C.S.da Silva, V.P.Brustein, Amaral Ferraz Navarro, F.A.dos Santos, L.C.Alves, M.G.dos Santos Cavalcanti, R.M.Srivastava, and M.das Graças Carneiro-Da-Cunha (2009).
Improved microwave-mediated synthesis of 3-(3-Aryl-1,2,4-oxadiazol-5-yl)propionic acids and their larvicidal and fungal growth inhibitory properties.
  Chem Pharm Bull (Tokyo), 57, 819-825.  
19288492 R.Maccari, R.Ottanà, R.Ciurleo, P.Paoli, G.Manao, G.Camici, C.Laggner, and T.Langer (2009).
Structure-based optimization of benzoic acids as inhibitors of protein tyrosine phosphatase 1B and low molecular weight protein tyrosine phosphatase.
  ChemMedChem, 4, 957-962.  
17139078 A.G.Evdokimov, M.Pokross, R.Walter, M.Mekel, B.Cox, C.Li, R.Bechard, F.Genbauffe, R.Andrews, C.Diven, B.Howard, V.Rastogi, J.Gray, M.Maier, and K.G.Peters (2006).
Engineering the catalytic domain of human protein tyrosine phosphatase beta for structure-based drug discovery.
  Acta Crystallogr D Biol Crystallogr, 62, 1435-1445.
PDB codes: 2hc1 2hc2 2i3r 2i3u 2i4e 2i4g 2i4h 2i5x
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