1tm0 | pdb_00001tm0
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Crystal Structure of the putative proline racemase from Brucella melitensis, Northeast Structural Genomics Target LR31
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Structural highlights
FunctionY1586_BRUME In vitro, catalyzes the epimerization of trans-4-hydroxy-L-proline (t4LHyp) to cis-4-hydroxy-D-proline (c4DHyp) and that of trans-3-hydroxy-L-proline (t3LHyp) to cis-3-hydroxy-D-proline (c3DHyp), albeit with very low efficiency. The physiological substrate may be different (PubMed:24980702). Displays neither proline racemase activity nor t3LHyp dehydratase activity (PubMed:17849014, PubMed:24980702).[1] [2] [3] Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. References
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This page was last modified 08:42, 1 May 2024.