1u2p Summary

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Crystal structure of Mycobacterium tuberculosis Low Molecular Protein Tyrosine Phosphatase (MPtpA) at 1.9A resolution

The structure was published by Madhurantakam, C., Rajakumara, E., Mazumdar, P.A., et al., Wiker, H.G., Sankaranarayanan, R., and Das, A.K., in 2005 in a paper entitled "Crystal Structure of Low-Molecular-Weight Protein Tyrosine Phosphatase from Mycobacterium tuberculosis at 1.9-A Resolution" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.9 Å and deposited in 2004.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of low molecular weight protein-tyrosine-phosphatase. This molecule has the UniProt identifier P9WIA1 (PTPA_MYCTU)search. The sample contained 163 residues which is 100% of the natural sequence. Out of 163 residues 156 were observed and are deposited in the PDB.

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 is most likely monomeric.

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):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A low molecular weight protein-tyrosine-phosphatase P9WIA1 (1-163) (PTPA_MYCTU)search Mycobacterium tuberculosis H37Rvsearch 100% 163 95%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P9WIA1 (1 - 163) low molecular weight protein-tyrosine-phosphatase Mycobacterium tuberculosis

Chain Structural classification (CATH)
A (P9WIA1) Rossmann foldsearch

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A (P9WIA1) protein dephosphorylationsearch peptidyl-tyrosine dephosphorylationsearch modification by symbiont of host morphology or physiology via secreted substancesearch negative regulation by symbiont of host cell-mediated immune responsesearch pathogenesissearch protein tyrosine phosphatase activitysearch protein bindingsearch phosphoprotein phosphatase activitysearch phosphatidylinositol-3-phosphatase activitysearch hydrolase activitysearch host cell endosomesearch extracellular regionsearch plasma membranesearch host cell cytoplasmsearch

Chain InterPro annotation
A Protein-tyrosine phosphatase/arsenate reductasesearch Protein-tyrosine phosphatase, low molecular weightsearch Phosphotyrosine protein phosphatase I superfamilysearch