1gpm | pdb_00001gpm

ESCHERICHIA COLI GMP SYNTHETASE COMPLEXED WITH AMP AND PYROPHOSPHATE

spinqualitylabelsall models 1gpm, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1gpm is a 4 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: AMP, CIT, MG, PO4, POP Gene: GUAA (ECOLI) Activity: GMP synthase (glutamine-hydrolyzing), with EC number 6.3.5.2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [GUAA_ECOLI] Catalyzes the synthesis of GMP from XMP.[HAMAP-Rule:MF_00344] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The crystal structure of GMP synthetase serves as a prototype for two families of metabolic enzymes. The Class I glutamine amidotransferase domain of GMP synthetase is found in related enzymes of the purine, pyrimidine, tryptophan, arginine, histidine and folic acid biosynthetic pathways. This domain includes a conserved Cys-His-Glu triad and is representative of a new family of enzymes that use a catalytic triad for enzymatic hydrolysis. The structure and conserved sequence fingerprint of the nucleotide-binding site in a second domain of GMP synthetase are common to a family of ATP pyrophosphatases, including NAD synthetase, asparagine synthetase and argininosuccinate synthetase. The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families.,Tesmer JJ, Klem TJ, Deras ML, Davisson VJ, Smith JL Nat Struct Biol. 1996 Jan;3(1):74-86. PMID:8548458 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also GMP synthase

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