3IJL
Structure of dipeptide epimerase from Bacteroides thetaiotaomicron complexed with L-Pro-D-Glu; nonproductive substrate binding.
Summary for 3IJL
Entry DOI | 10.2210/pdb3ijl/pdb |
Related | 3IJI 3IJQ |
Descriptor | Muconate cycloisomerase, PROLINE, D-GLUTAMIC ACID, ... (5 entities in total) |
Functional Keywords | enolase superfamily, dipeptide epimerase, l-pro-d-glu, nonproductive binding, isomerase |
Biological source | Bacteroides thetaiotaomicron |
Total number of polymer chains | 2 |
Total formula weight | 75639.87 |
Authors | Fedorov, A.A.,Fedorov, E.V.,Lukk, T.,Gerlt, J.A.,Almo, S.C. (deposition date: 2009-08-04, release date: 2010-07-21, Last modification date: 2023-09-06) |
Primary citation | Lukk, T.,Sakai, A.,Kalyanaraman, C.,Brown, S.D.,Imker, H.J.,Song, L.,Fedorov, A.A.,Fedorov, E.V.,Toro, R.,Hillerich, B.,Seidel, R.,Patskovsky, Y.,Vetting, M.W.,Nair, S.K.,Babbitt, P.C.,Almo, S.C.,Gerlt, J.A.,Jacobson, M.P. Homology models guide discovery of diverse enzyme specificities among dipeptide epimerases in the enolase superfamily. Proc.Natl.Acad.Sci.USA, 109:4122-4127, 2012 Cited by PubMed: 22392983DOI: 10.1073/pnas.1112081109 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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