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Ligands
Code Name Style Show Link
F20 N-benzoyl-L-phenylalanyl-4-[(5s)-1,1-dioxido-3-oxoisothiazolidin-5-yl]-L-phenylalaninamide
Non-standard Residues
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Glycosylation
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Code : 2CMA   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : Structural Basis for Inhibition of Protein Tyrosine Phosphatase 1B by Isothiazolidinone Heterocyclic Phosphonate Mimetics
Release Data : 2006-08-17
Compound :
mol_id molecule chains synonym
1 TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 1 A PROTEIN TYROSINE PHOSPHATASE 1B, PTP-1B
ec: 3.1.3.48
fragment: CATALYTIC DOMAIN, RESIDUES 1-321
Source :
mol_id organism_scientific organism_common expression_system
1 HOMO SAPIENS  (taxid:9606) HUMAN ESCHERICHIA COLI  (taxid:469008)
expression_system_strain: BL21(DE3)
Authors : Ala, P.J., Gonneville, L., Hillman, M.C., Becker-Pasha, M., Wei, M., Reid, B.G., Klabe, R., Yue, E.W., Wayland, B., Douty, B., Combs, A.P., Polam, P., Wasserman, Z., Bower, M., Burn, T.C., Hollis, G.F., Wynn, R.
Keywords : POLYMORPHISM, PHOSPHORYLATION, PROTEIN PHOSPHATASE, ENDOPLASMIC RETICULUM, OXIDATION, HYDROLASE, ACETYLATION, PHOSPHATASE
Exp. method : X-RAY DIFFRACTION ( 2.3 Å )
Citation :

Structural Basis for Inhibition of Protein-Tyrosine Phosphatase 1B by Isothiazolidinone Heterocyclic Phosphonate Mimetics.

Ala, P.J.,Gonneville, L.,Hillman, M.C.  et al.
(2006)  J.Biol.Chem.  281 : 32784

PubMed: 16916797
DOI: 10.1074/JBC.M606873200

Chain : A
UniProt : P18031 (PTN1_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate 3.1.3.48 PROSITE- ProRule:PRU10044
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