5LHT
ATP Phosphoribosyltransferase from Mycobacterium tuberculosis in complex with the allosteric activator 3-(2-Thienyl)-L-alanine
Summary for 5LHT
Entry DOI | 10.2210/pdb5lht/pdb |
Descriptor | ATP phosphoribosyltransferase, BETA(2-THIENYL)ALANINE, SULFATE ION, ... (5 entities in total) |
Functional Keywords | atp-prtase, act, his g, histidine biosynthesis, transferase |
Biological source | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
Cellular location | Cytoplasm : P9WMN1 |
Total number of polymer chains | 1 |
Total formula weight | 32333.59 |
Authors | de Chiara, C.,Pisco, J.P.,de Carvalho, L.P.,Smerdon, S.J.,Walker, P.A.,Ogrodowicz, R. (deposition date: 2016-07-12, release date: 2017-07-05, Last modification date: 2024-01-10) |
Primary citation | Pisco, J.P.,Chiara, C.,Pacholarz, K.J.,Garza-Garcia, A.,Ogrodowicz, R.W.,Walker, P.A.,Barran, P.E.,Smerdon, S.J.,Carvalho, L.P.S. Uncoupling conformational states from activity in an allosteric enzyme. Nat Commun, 8:203-203, 2017 Cited by PubMed: 28781362DOI: 10.1038/s41467-017-00224-0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.0601 Å) |
Structure validation
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