3IVA

Structure of the B12-dependent Methionine Synthase (MetH) C-teminal half with AdoHcy bound

Summary for 3IVA

Entry DOI	10.2210/pdb3iva/pdb
Related	1K7Y 3BUL 3IV9
Descriptor	Methionine synthase, COBALAMIN, S-ADENOSYL-L-HOMOCYSTEINE, ... (5 entities in total)
Functional Keywords	meth, transferase, reactivation conformation, h759, cobalamin, intermodular interactions, amino-acid biosynthesis, cobalt, metal-binding, methionine biosynthesis, methyltransferase, s-adenosyl-l-methionine, s-adenosyl-homocysteine
Biological source	Escherichia coli
Total number of polymer chains	1
Total formula weight	67138.29
Authors	Pattridge, K.A.,Koutmos, M.,Smith, J.L. (deposition date: 2009-08-31, release date: 2009-11-24, Last modification date: 2023-09-06)
Primary citation	Koutmos, M.,Datta, S.,Pattridge, K.A.,Smith, J.L.,Matthews, R.G. Insights into the reactivation of cobalamin-dependent methionine synthase. Proc.Natl.Acad.Sci.USA, 106:18527-18532, 2009 Cited by PubMed: 19846791 DOI: 10.1073/pnas.0906132106 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.7 Å)

Structure validation