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3IV9

Structure of the B12-dependent Methionine Synthase (MetH) C-teminal half in a "His-On" conformation

Summary for 3IV9
Entry DOI10.2210/pdb3iv9/pdb
Related1K7Y 3BUL 3IVA
DescriptorMethionine synthase, COBALAMIN (3 entities in total)
Functional Keywordsmeth, transferase, reactivation conformation, h759, cobalamin, intermodular interactions, amino-acid biosynthesis, cobalt, metal-binding, methionine biosynthesis, methyltransferase, s-adenosyl-l-methionine
Biological sourceEscherichia coli
Total number of polymer chains1
Total formula weight66505.86
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 citationKoutmos, 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 (3.25 Å)
Structure validation

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