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4DZ4

X-ray crystal structure of a hypothetical Agmatinase from Burkholderia thailandensis

Summary for 4DZ4
Entry DOI10.2210/pdb4dz4/pdb
DescriptorAgmatinase, MANGANESE (II) ION, 1,2-ETHANEDIOL, ... (5 entities in total)
Functional Keywordsagmatinase, hydrolase, structural genomics, seattle structural genomics center for infectious disease, ssgcid
Biological sourceBurkholderia thailandensis
Total number of polymer chains6
Total formula weight214043.47
Authors
Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2012-02-29, release date: 2012-03-28, Last modification date: 2025-02-12)
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 (1.7 Å)
Structure validation

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