Summary for 6CNZ
Entry DOI | 10.2210/pdb6cnz/pdb |
Descriptor | Chorismate mutase, NITRATE ION, 1,2-ETHANEDIOL, ... (4 entities in total) |
Functional Keywords | ssgcid, chorismate mutase, structural genomics, seattle structural genomics center for infectious disease, isomerase |
Biological source | Burkholderia thailandensis |
Total number of polymer chains | 6 |
Total formula weight | 117777.24 |
Authors | Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2018-03-09, release date: 2018-03-21, Last modification date: 2024-10-09) |
Primary citation | Asojo, O.A.,Dranow, D.M.,Serbzhinskiy, D.,Subramanian, S.,Staker, B.,Edwards, T.E.,Myler, P.J. Crystal structure of chorismate mutase from Burkholderia thailandensis. Acta Crystallogr F Struct Biol Commun, 74:294-299, 2018 Cited by PubMed Abstract: Burkholderia thailandensis is often used as a model for more virulent members of this genus of proteobacteria that are highly antibiotic-resistant and are potential agents of biological warfare that are infective by inhalation. As part of ongoing efforts to identify potential targets for the development of rational therapeutics, the structures of enzymes that are absent in humans, including that of chorismate mutase from B. thailandensis, have been determined by the Seattle Structural Genomics Center for Infectious Disease. The high-resolution structure of chorismate mutase from B. thailandensis was determined in the monoclinic space group P2 with three homodimers per asymmetric unit. The overall structure of each protomer has the prototypical AroQγ topology and shares conserved binding-cavity residues with other chorismate mutases, including those with which it has no appreciable sequence identity. PubMed: 29717997DOI: 10.1107/S2053230X1800506X PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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