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3gar
From Proteopedia
A PH-DEPENDENT STABLIZATION OF AN ACTIVE SITE LOOP OBSERVED FROM LOW AND HIGH PH CRYSTAL STRUCTURES OF MUTANT MONOMERIC GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE
Template:ABSTRACT PUBMED 9698564
About this Structure
3GAR is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
A pH-dependent stabilization of an active site loop observed from low and high pH crystal structures of mutant monomeric glycinamide ribonucleotide transformylase at 1.8 to 1.9 A., Su Y, Yamashita MM, Greasley SE, Mullen CA, Shim JH, Jennings PA, Benkovic SJ, Wilson IA, J Mol Biol. 1998 Aug 21;281(3):485-99. PMID:9698564
Page seeded by OCA on Sun Jul 27 17:15:24 2008
Categories: Escherichia coli | Phosphoribosylglycinamide formyltransferase | Single protein | Benkovic, S J. | Greasley, S E. | Jennings, P A. | Mullen, C A. | Shim, J H. | Su, Y. | Wilson, I A. | Yamashita, M M. | Anti-cancer agent | Enzyme mechanism | Folate cofactor | Loop flexibility | Monomer-dimer association | Purine biosynthesis
