1YDN
Crystal Structure of the HMG-CoA Lyase from Brucella melitensis, Northeast Structural Genomics Target LR35.
Summary for 1YDN
Entry DOI | 10.2210/pdb1ydn/pdb |
Related | 1YDO |
Descriptor | HYDROXYMETHYLGLUTARYL-COA LYASE, CALCIUM ION (3 entities in total) |
Functional Keywords | tim-barrel protein, structural genomics, psi, protein structure initiative, northeast structural genomics consortium, nesg, lyase |
Biological source | Brucella melitensis |
Total number of polymer chains | 4 |
Total formula weight | 126711.86 |
Authors | Forouhar, F.,Abashidze, M.,Hussain, M.,Vorobiev, S.M.,Xiao, R.,Ciano, M.,Acton, T.B.,Montelione, G.T.,Tong, L.,Hunt, J.F.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2004-12-24, release date: 2005-07-05, Last modification date: 2017-10-11) |
Primary citation | Forouhar, F.,Hussain, M.,Farid, R.,Benach, J.,Abashidze, M.,Edstrom, W.C.,Vorobiev, S.M.,Xiao, R.,Acton, T.B.,Fu, Z.,Kim, J.J.,Miziorko, H.M.,Montelione, G.T.,Hunt, J.F. Crystal structures of two bacterial 3-hydroxy-3-methylglutaryl-CoA lyases suggest a common catalytic mechanism among a family of TIM barrel metalloenzymes cleaving carbon-carbon bonds. J.Biol.Chem., 281:7533-7545, 2006 Cited by PubMed: 16330546DOI: 10.1074/jbc.M507996200 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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