4REQ

Methylmalonyl-COA Mutase substrate complex

Summary for 4REQ

Entry DOI	10.2210/pdb4req/pdb
Descriptor	METHYLMALONYL-COA MUTASE, COBALAMIN, SUCCINYL-COENZYME A, ... (8 entities in total)
Functional Keywords	isomerase, mutase, intramolecular transferase
Biological source	Propionibacterium freudenreichii subsp. shermanii More
Total number of polymer chains	4
Total formula weight	306138.08
Authors	Evans, P.R.,Mancia, F. (deposition date: 1998-06-17, release date: 1999-01-13, Last modification date: 2024-05-22)
Primary citation	Mancia, F.,Evans, P.R. Conformational changes on substrate binding to methylmalonyl CoA mutase and new insights into the free radical mechanism. Structure, 6:711-720, 1998 Cited by PubMed Abstract: Methylmalonyl CoA mutase catalyses the interconversion of succinyl CoA and methylmalonyl CoA via a free radical mechanism. The enzyme belongs to a family of enzymes that catalyse intramolecular rearrangement reactions in which a group and a hydrogen atom on adjacent carbons are exchanged. These enzymes use the cofactor adenosylcobalamin (coenzyme B12) which breaks to form an adenosyl radical, thus initiating the reaction. Determination of the structure of substrate-free methylmalonyl CoA mutase was initiated to provide further insight into the mechanism of radical formation. PubMed: 9655823 DOI: 10.1016/S0969-2126(98)00073-2 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.2 Å)

Structure validation