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Kinetic and Structural Studies of the Low Moleuclar Weight Protein Tyrosine Phosphatase from Tritrichomonas foetus
Authors
Thomas, C.L., Hallenga, K., Stauffacher, C.V., Van Etten, R.L.
Assembly
protein tyrosine phosphatase (E.C.3.1.3.48)
Entity
1. protein tyrosine phosphatase (E.C.3.1.3.48) (polymer, Thiol state: all free), 146 monomers, 15820.99 Da Detail

AAEKKAVLFV CLGNICRSPA CEGICRDMVG DKLIIDSAAT SGFHVGQSPD TRSQKVCKSN GVDISKQRAR QITKADFSKF DVIAALDQSI LSDINSMKPS NCRAKVVLFN PPNGVDDPYY SSDGFPTMFA SISKEMKPFL TEHGLI


Formula weight
15820.99 Da
Source organism
Tritrichomonas foetus
Exptl. method
NMR
Refine. method
simulated annealing
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 100.0 %, Completeness: 81.2 %, Completeness (bb): 82.7 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All81.2 % (1343 of 1653)86.9 % (747 of 860)69.7 % (449 of 644)98.7 % (147 of 149)
Backbone82.7 % (711 of 860)98.6 % (289 of 293)66.7 % (286 of 429)98.6 % (136 of 138)
Sidechain82.2 % (764 of 930)80.8 % (458 of 567)83.8 % (295 of 352)100.0 % (11 of 11)
Aromatic43.3 % (45 of 104)51.9 % (27 of 52)34.6 % (18 of 52)
Methyl98.7 % (148 of 150)98.7 % (74 of 75)98.7 % (74 of 75)

1. protein tyrosine phosphatase (E.C.3.1.3.48)

AAEKKAVLFV CLGNICRSPA CEGICRDMVG DKLIIDSAAT SGFHVGQSPD TRSQKVCKSN GVDISKQRAR QITKADFSKF DVIAALDQSI LSDINSMKPS NCRAKVVLFN PPNGVDDPYY SSDGFPTMFA SISKEMKPFL TEHGLI

Sample

Pressure 1 atm, Temperature 298 K, pH 5.2


#NameIsotope labelingTypeConcentration
1protein tyrosine phosphatase (E.C.3.1.3.48)[U-15N; U-13C]1.0 ~ 2.0 mM
2NaCl130 mM
3NaH2PO420 mM
4DSS1 mM
5H2090 %
6D2O10 %

Protein Blocks Logo
Calculated from 21 models in PDB: 1P8A, Strand ID: A Detail


Release date
2004-05-14
Citation 1
Solution structure of the low-molecular-weight protein tyrosine phosphatase from Tritrichomonas foetus reveals a flexible phosphate binding loop
Gustafson, C.L.T., Stauffacher, C.V., Hallenga, K., Van Etten, R.L.
Protein Sci. (2005), 14, 2515-2525, PubMed 16195543 , DOI 10.1110/ps.051618805 ,
Citation 2
Kinetic and spectroscopic studies of Tritrichomonas foetus low-molecular weight phosphotyrosyl phosphatase. Hydrogen bond networks and electrostatic effects
Thomas, C.L., McKinnon, E., Granger, B.L., Harms, E., Van Etten, R.L.
Biochemistry (2002), 41, 15601-15609, PubMed 12501188 , DOI: ,
Related entities 1. protein tyrosine phosphatase (E.C.3.1.3.48), : 1 : 103 entities Detail
Experiments performed 3 experiments Detail
nullKeywords low molecular weight protein tyrosine phosphatase, Tritrichomonas foetus