CRYSTAL STRUCTURE OF A YEAST LOW MOLECULAR WEIGHT PROTEIN TYROSINE PHOSPHATASE (LTP1) COMPLEXED WITH THE ACTIVATOR ADENINE
The structure was published by Wang, S., Stauffacher, C.V., and Van Etten, R.L., in 2000 in a paper entitled "Structural and mechanistic basis for the activation of a low-molecular weight protein tyrosine phosphatase by adenine." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.9 Å and deposited in 1999.
The experimental data on which the structure is based was also deposited.
This PDB entry contains multiple copies of the structure of TYROSINE PHOSPHATASE.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 1 unique UniProt protein: