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PDBe Entry: 2p50 view

Crystal structure of N-acetyl-D-Glucosamine-6-Phosphate deacetylase liganded with Zn
Summary
Header HYDROLASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 2.2 Å, R-factor: 21.2%, Free R-factor: 25.7%, Spacegroup: C 2 2 21
Released 24/07/2007, deposition: 14/03/2007, last revision: 24/02/2009
Authors Fedorov, A.A.search; Fedorov, E.V.search; Hall, R.S.search; Raushel, F.M.search; Almo, S.C.search
Primary citation Structural Diversity within the Mononuclear and Binuclear Active Sites of N-Acetyl-d-glucosamine-6-phosphate Deacetylase.
BIOCHEMISTRYsearch vol:46, pag:7953-7962 (2007) [PubMed ID 17567048 ]search
Keywords N-acetyl-d-glucosamine-6-phosphate deacetylasesearch, amidohydrolasesearch, (beta/alpha)8-barrelsearch
EC 3.5.1.25 ExPASy BRENDA search (A B C D)
Organism Escherichia coli K-12 83333search(A B C D)
UniProt N-acetylglucosamine-6-phosphate deacetylase (EC 3.5.1.25) (GlcNAc 6-P deacetylase) P0AF18search (A B C D)
Solvent A, B, C, D
Related entries 1ymy, 2p53
Polymers
Id Name Type UniProt Residues Observed
A, B, C, D N-acetylglucosamine-6-phosphate deacetylase Protein P0AF18 (NAGA_ECOLI)search
382 100%
Heterogens
Id Name Ligands
A, B, C, D ZINC ION ZN search
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