PDBsum entry 2f71

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Hydrolase PDB id
Protein chain
297 a.a. *
_CL ×4
Waters ×348
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Protein tyrosine phosphatase 1b with sulfamic acid inhibitor
Structure: Tyrosine-protein phosphatase, non-receptor type 1 chain: a. Fragment: catalytic domain, residues 1-298. Synonym: protein-tyrosine phosphatase 1b, ptp-1b. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: ptpn1, ptp1b. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
1.55Å     R-factor:   0.153     R-free:   0.172
Authors: A.G.Evdokimov,M.E.Pokross,S.R.Klopfenstein
Key ref: S.R.Klopfenstein et al. (2006). 1,2,3,4-Tetrahydroisoquinolinyl sulfamic acids as phosphatase PTP1B inhibitors. Bioorg Med Chem Lett, 16, 1574-1578. PubMed id: 16386905 DOI: 10.1016/j.bmcl.2005.12.051
29-Nov-05     Release date:   13-Dec-05    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P18031  (PTN1_HUMAN) -  Tyrosine-protein phosphatase non-receptor type 1
435 a.a.
297 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 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
Bound ligand (Het Group name = UN7)
matches with 40.00% similarity
+ 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.2005.12.051 Bioorg Med Chem Lett 16:1574-1578 (2006)
PubMed id: 16386905  
1,2,3,4-Tetrahydroisoquinolinyl sulfamic acids as phosphatase PTP1B inhibitors.
S.R.Klopfenstein, A.G.Evdokimov, A.O.Colson, N.T.Fairweather, J.J.Neuman, M.B.Maier, J.L.Gray, G.S.Gerwe, G.E.Stake, B.W.Howard, J.A.Farmer, M.E.Pokross, T.R.Downs, B.Kasibhatla, K.G.Peters.
High-throughput screening of the P&GP corporate repository against several protein tyrosine phosphatases identified the sulfamic acid moiety as potential phosphotyrosine mimetic. Incorporation of the sulfamic acid onto a 1,2,3,4-tetrahydroisoquinoline scaffold provided a promising starting point for PTP1B inhibitor design.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20727982 C.Abad-Zapatero, O.Perišić, J.Wass, A.P.Bento, J.Overington, B.Al-Lazikani, and M.E.Johnson (2010).
Ligand efficiency indices for an effective mapping of chemico-biological space: the concept of an atlas-like representation.
  Drug Discov Today, 15, 804-811.  
19810703 D.Vidović, and S.C.Schürer (2009).
Knowledge-based characterization of similarity relationships in the human protein-tyrosine phosphatase family for rational inhibitor design.
  J Med Chem, 52, 6649-6659.  
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.  
19729231 S.Cheng, X.Zhang, W.Wang, M.Zhao, M.Zheng, H.W.Chang, J.Wu, and S.Peng (2009).
A class of novel N-(3S-1,2,3,4-tetrahydroisoquinoline-3-carbonyl)-L-amino acid derivatives: their synthesis, anti-thrombotic activity evaluation, and 3D QSAR analysis.
  Eur J Med Chem, 44, 4904-4919.  
17543532 R.Maccari, P.Paoli, R.Ottanà, M.Jacomelli, R.Ciurleo, G.Manao, T.Steindl, T.Langer, M.G.Vigorita, and G.Camici (2007).
5-Arylidene-2,4-thiazolidinediones as inhibitors of protein tyrosine phosphatases.
  Bioorg Med Chem, 15, 5137-5149.  
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