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EBI PDBe PDBeView

PDBe Entry: 2oi5 view

E. coli GlmU- Complex with UDP-GlcNAc and Acetyl-CoA
Summary
Header TRANSFERASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 2.25 Å, R-factor: 17.8%, Free R-factor: 21.9%, Spacegroup: H 3 2
Released 19/06/2007, deposition: 10/01/2007, last revision: 24/02/2009
Authors Olsen, L.R.search; Vetting, M.W.search; Roderick, S.L.search
Primary citation Structure of the E. coli bifunctional GlmU acetyltransferase active site with substrates and products.
PROTEIN SCI.search vol:16, pag:1230-1235 (2007) [PubMed ID 17473010 ]search
Keywords LEFT-HANDED BETA HELIXsearch, TRANSFERASEsearch
EC 2.3.1.157 ExPASy BRENDA search 2.7.7.23 ExPASy BRENDA search (A B)
Organism Escherichia coli 562search(A B)
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)] P0ACC7search (A B)
Solvent A, B
Related entries 1hv9, 2oi6, 2oi7
Polymers
Id Name Type UniProt Residues Observed
A, B Bifunctional protein glmU Protein P0ACC7 (GLMU_ECOLI)search
 456 98%
Heterogens
Id Name Ligands
B, A MAGNESIUM ION MG search
A, B SULFATE ION SO4 search
A, B ACETYL COENZYME *A ACO search
A, B URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE UD1 search
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