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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 DOI10.2210/pdb3gar/pdb
DescriptorGLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE, PHOSPHATE ION (3 entities in total)
Functional Keywordspurine biosynthesis, folate cofactors, loop flexibility, monomer-dimer association, enzyme mechanism, anti-cancer agents
Biological sourceEscherichia coli
Total number of polymer chains1
Total formula weight23303.19
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: 2023-08-09)
Primary citationSu, 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: 9698564
DOI: 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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