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PDBe Entry: 1g95 view

CRYSTAL STRUCTURE OF S.PNEUMONIAE GLMU, APO FORM
Summary
Header TRANSFERASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 2.33 Å, R-factor: 22.8%, Free R-factor: 30.3%, Spacegroup: H 3 2
Released 22/05/2001, deposition: 22/11/2000, last revision: 24/02/2009
Authors Kostrewa, D.search; D'Arcy, A.search; Kamber, M.search
Primary citation Crystal structures of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase, GlmU, in apo form at 2.33 A resolution and in complex with UDP-N-acetylglucosamine and Mg(2+) at 1.96 A resolution.
J.MOL.BIOL.search vol:305, pag:279-289 (2001) [PubMed ID 11124906 ]search
Keywords GlmUsearch, Acetyltransferasesearch, uridyltransferase pyrophosphorylasesearch, left-handed beta-sheet helixsearch, trimersearch
EC 2.3.1.157 ExPASy BRENDA search 2.7.7.23 ExPASy BRENDA search (A)
Organism Streptococcus pneumoniae 1313search(A)
UniProt Bifunctional protein glmU [Includes: UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase); Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157)] Q97R46search (A)
Solvent A
Related entries 1g97
Polymers
Id Name Type UniProt Residues Observed
A N-ACETYLGLUCOSAMINE-1-PHOSPHATE URIDYLTRANSFERASE Protein Q97R46 (GLMU_STRPN)search
459 96%
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