EC 5.1.99.4 - 2- methylacyl- CoA 2- epimerase (\xCE\xB1- methylacyl- CoA racemase)
3D structures of EC 5.1.99.4 - \xCE\xB1-methylacyl-CoA racemase in Protein Data Bank
updated: 6 January 2022, 2:15
In total: 8 PDB structures of EC 5.1.99.4 - \xCE\xB1-methylacyl-CoA racemase:
- 1x74: Alpha-methylacyl-coa Racemase from Mycobacterium Tuberculosis- Mutational and Structural Characterization of The Fold and Active Site
- 2g04: Crystal Structure of Fatty Acid-coa Racemase from Mycobacterium Tuberculosis H37RV
- 2gce: The 1,1-proton Transfer Reaction Mechanism by Alpha- Methylacyl-coa Racemase Is Catalyzed by an Aspartate/histidine Pair and Involves a Smooth, Methionine- Rich Surface for Binding The Fatty Acyl Moiety
- 2gci: The 1,1-proton Transfer Reaction Mechanism by Alpha- Methylacyl-coa Racemase Is Catalyzed by an Asparte/histidine Pair and Involves a Smooth, Methionine- Rich Surface for Binding The Fatty Acyl Moiety
- 2gd0: The 1,1-proton Transfer Reaction Mechanism by Alpha- Methylacyl-coa Racemase Is Catalyzed by an Aspartate/histidine Pair and Involves a Smooth, Methionine- Rich Surface for Binding The Fatty Acyl Moiety
- 2gd2: The 1,1-proton Transfer Reaction Mechanism by Alpha- Methylacyl-coa Racemase Is Catalyzed by an Aspartate/histidine Pair and Involves a Smooth, Methionine- Rich Surface for Binding The Fatty Acyl Moiety
- 2gd6: The 1,1-proton Transfer Reaction Mechanism by Alpha- Methylacyl-coa Racemase Is Catalyzed by an Aspartate/histidine Pair and Involves a Smooth, Methionine- Rich Surface for Binding The Fatty Acyl Moiety
- 2yim: The Enolisation Chemistry of a Thioester-dependent Racemase: The 1.4 a Crystal Structure of a Complex with a Planar Reaction Intermediate Analogue
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