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3IJQ

Structure of dipeptide epimerase from Bacteroides thetaiotaomicron complexed with L-Ala-D-Glu; productive substrate binding.

Summary for 3IJQ
Entry DOI10.2210/pdb3ijq/pdb
Related3IJI 3IJL
DescriptorMuconate cycloisomerase, ALANINE, D-GLUTAMIC ACID, ... (6 entities in total)
Functional Keywordsenolase superfamily, dipeptide epimerase, l-ala-d-glu, productive binding, isomerase
Biological sourceBacteroides thetaiotaomicron
Total number of polymer chains2
Total formula weight75683.86
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 citationLukk, 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: 22392983
DOI: 10.1073/pnas.1112081109
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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