3GAR
A PH-DEPENDENT STABLIZATION OF AN ACTIVE SITE LOOP OBSERVED FROM LOW AND HIGH PH CRYSTAL STRUCTURES OF MUTANT MONOMERIC GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE
Summary for 3GAR
Entry DOI | 10.2210/pdb3gar/pdb |
Descriptor | GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE, PHOSPHATE ION (3 entities in total) |
Functional Keywords | purine biosynthesis, folate cofactors, loop flexibility, monomer-dimer association, enzyme mechanism, anti-cancer agents |
Biological source | Escherichia coli |
Total number of polymer chains | 1 |
Total formula weight | 23303.19 |
Authors | Su, Y.,Yamashita, M.M.,Greasley, S.E.,Mullen, C.A.,Shim, J.H.,Jennings, P.A.,Benkovic, S.J.,Wilson, I.A. (deposition date: 1998-05-13, release date: 1998-08-12, Last modification date: 2024-05-22) |
Primary citation | Su, Y.,Yamashita, M.M.,Greasley, S.E.,Mullen, C.A.,Shim, J.H.,Jennings, P.A.,Benkovic, S.J.,Wilson, I.A. 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. J.Mol.Biol., 281:485-499, 1998 Cited by PubMed: 9698564DOI: 10.1006/jmbi.1998.1931 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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