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
Summary for 2GCI
Entry DOI | 10.2210/pdb2gci/pdb |
Related | 1X74 2GCE 2GD0 2GD2 2GD6 |
Descriptor | probable alpha-methylacyl-CoA racemase MCR, (R)-2-METHYLMYRISTOYL-COENZYME A, GLYCEROL, ... (4 entities in total) |
Functional Keywords | alpha-methylacyl-coa racemase, racemase, coa transferase, proton transfer, coenzyme a, isomerase |
Biological source | Mycobacterium tuberculosis |
Total number of polymer chains | 4 |
Total formula weight | 159411.43 |
Authors | Bhaumik, P.,Wierenga, R.K. (deposition date: 2006-03-14, release date: 2007-02-20, Last modification date: 2023-10-25) |
Primary citation | Bhaumik, P.,Schmitz, W.,Hassinen, A.,Hiltunen, J.K.,Conzelmann, E.,Wierenga, R.K. The Catalysis of the 1,1-Proton Transfer by alpha-Methyl-acyl-CoA Racemase Is Coupled to a Movement of the Fatty Acyl Moiety Over a Hydrophobic, Methionine-rich Surface J.Mol.Biol., 367:1145-1161, 2007 Cited by PubMed: 17320106DOI: 10.1016/j.jmb.2007.01.062 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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