2KOK
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![BU of 2kok by Molmil](/molmil-images/mine/2kok) | Solution structure of an arsenate reductase (ArsC) related protein from Brucella melitensis. Seattle Structural Genomics Center for Infectious Disease target BrabA.00007.a. | Descriptor: | arsenate reductase | Authors: | Buchko, G.W, Hewitt, S.N, Napuli, A.J, Van Voorhis, W.C, Seattle Structural Genomics Center for Infectious Disease (SSGCID) | Deposit date: | 2009-09-23 | Release date: | 2009-10-13 | Last modified: | 2024-05-08 | Method: | SOLUTION NMR | Cite: | Solution structure of an arsenate reductase-related protein, YffB, from Brucella melitensis, the etiological agent responsible for brucellosis. Acta Crystallogr.,Sect.F, 67, 2011
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2KN9
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![BU of 2kn9 by Molmil](/molmil-images/mine/2kn9) | Solution structure of zinc-substituted rubredoxin B (Rv3250c) from Mycobacterium tuberculosis. Seattle Structural Genomics Center for Infectious Disease target MytuD.01635.a | Descriptor: | Rubredoxin, ZINC ION | Authors: | Buchko, G.W, Hewitt, S.N, Napuli, A.J, Van Voorhis, W.C, Seattle Structural Genomics Center for Infectious Disease (SSGCID) | Deposit date: | 2009-08-20 | Release date: | 2009-09-15 | Last modified: | 2024-05-01 | Method: | SOLUTION NMR | Cite: | Solution-state NMR structure and biophysical characterization of zinc-substituted rubredoxin B (Rv3250c) from Mycobacterium tuberculosis. Acta Crystallogr.,Sect.F, 67, 2011
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3GMT
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![BU of 3gmt by Molmil](/molmil-images/mine/3gmt) | Crystal structure of adenylate kinase from burkholderia pseudomallei | Descriptor: | Adenylate kinase, SULFATE ION | Authors: | Abendroth, J, Staker, B.L, Robinson, H, Buchko, G.W, Hewitt, S.N, Napuli, A.J, Van Voorhis, W, Stacy, R, Myler, P.J, Stewart, L, Seattle Structural Genomics Center for Infectious Disease (SSGCID) | Deposit date: | 2009-03-15 | Release date: | 2009-06-02 | Last modified: | 2013-10-30 | Method: | X-RAY DIFFRACTION (2.1 Å) | Cite: | Structural characterization of Burkholderia pseudomallei adenylate kinase (Adk): profound asymmetry in the crystal structure of the 'open' state. Biochem.Biophys.Res.Commun., 394, 2010
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