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PDBe Entry: 3gar 
A PH-DEPENDENT STABLIZATION OF AN ACTIVE SITE LOOP OBSERVED FROM LOW AND HIGH PH CRYSTAL STRUCTURES OF MUTANT MONOMERIC GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE
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PURINE BIOSYNTHESIS
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X-RAY DIFFRACTION
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Resolution: 1.9 Å, R-factor: 21.5%, Free R-factor: 27.4%, Spacegroup: P 61 2 2
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12/08/1998, deposition: 13/05/1998, last revision: 24/02/2009
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Su, Y.; Yamashita, M.M.; Greasley, S.E.; Mullen, C.A.; Shim, J.H.; Jennings, P.A.; Benkovic, S.J.; Wilson, I.A.
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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. vol:281, pag:485-499 (1998) [PubMed ID 9698564 ]
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PURINE BIOSYNTHESIS, FOLATE COFACTORS, LOOP FLEXIBILITY, MONOMER-DIMER ASSOCIATION, ENZYME MECHANISM, ANTI-CANCER AGENTS
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2.1.2.2 ExPASy BRENDA (A)
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Escherichia coli 562(A)
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Phosphoribosylglycinamide formyltransferase (EC 2.1.2.2) (5'-phosphoribosylglycinamide transformylase) (GAR transformylase) (GART) P08179 (A)
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A
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| A |
GLYCINAMIDE RIBONUCLEOTIDE TRANSFORMYLASE |
Protein |
P08179 (PUR3_ECOLI)
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212 |
98% |
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| A |
PHOSPHATE ION |
PO4
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