This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3iv9
From Proteopedia
Structure of the B12-dependent Methionine Synthase (MetH) C-teminal half in a "His-On" conformation
Template:ABSTRACT PUBMED 19846791
About this Structure
3IV9 is a 1 chain structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
- Koutmos M, Datta S, Pattridge KA, Smith JL, Matthews RG. Insights into the reactivation of cobalamin-dependent methionine synthase. Proc Natl Acad Sci U S A. 2009 Nov 3;106(44):18527-32. Epub 2009 Oct 21. PMID:19846791
Page seeded by OCA on Wed Nov 25 09:43:12 2009
Categories: Escherichia coli | Methionine synthase | Koutmos, M. | Pattridge, K A. | Smith, J L. | Amino-acid biosynthesis | Cobalamin | Cobalt | H759 | Intermodular interaction | Metal-binding | Meth | Methionine biosynthesis | Methyltransferase | Reactivation conformation | S-adenosyl-l-methionine | Transferase | Zinc
