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3UPT

Crystal structure of a transketolase from Burkholderia pseudomallei bound to TPP, calcium and ribose-5-phosphate

Summary for 3UPT
Entry DOI10.2210/pdb3upt/pdb
Related3UK1
DescriptorTransketolase, CALCIUM ION, THIAMINE DIPHOSPHATE, ... (6 entities in total)
Functional Keywordsstructural genomics, seattle structural genomics center for infectious disease, ssgcid, tpp, calcium-dependent, co-factor, e pentose phosphate pathway, calvin cycle, tkt, transferase
Biological sourceBurkholderia thailandensis
Total number of polymer chains2
Total formula weight155165.57
Authors
Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2011-11-18, release date: 2011-12-14, Last modification date: 2023-09-13)
Primary citationBaugh, L.,Gallagher, L.A.,Patrapuvich, R.,Clifton, M.C.,Gardberg, A.S.,Edwards, T.E.,Armour, B.,Begley, D.W.,Dieterich, S.H.,Dranow, D.M.,Abendroth, J.,Fairman, J.W.,Fox, D.,Staker, B.L.,Phan, I.,Gillespie, A.,Choi, R.,Nakazawa-Hewitt, S.,Nguyen, M.T.,Napuli, A.,Barrett, L.,Buchko, G.W.,Stacy, R.,Myler, P.J.,Stewart, L.J.,Manoil, C.,Van Voorhis, W.C.
Combining functional and structural genomics to sample the essential Burkholderia structome.
Plos One, 8:e53851-e53851, 2013
Cited by
PubMed Abstract: The genus Burkholderia includes pathogenic gram-negative bacteria that cause melioidosis, glanders, and pulmonary infections of patients with cancer and cystic fibrosis. Drug resistance has made development of new antimicrobials critical. Many approaches to discovering new antimicrobials, such as structure-based drug design and whole cell phenotypic screens followed by lead refinement, require high-resolution structures of proteins essential to the parasite.
PubMed: 23382856
DOI: 10.1371/journal.pone.0053851
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

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数据于2024-11-13公开中

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