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PDBe Entry: 2c1g view

STRUCTURE OF STREPTOCOCCUS PNEUMONIAE PEPTIDOGLYCAN DEACETYLASE (SPPGDA)
Summary
Header HYDROLASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 1.75 Å, R-factor: 21.1%, Free R-factor: 24.2%, Spacegroup: P 21 21 21
Released 15/09/2005, deposition: 14/09/2005, last revision: 24/02/2009
Authors Blair, D.E.search; Schuttelkopf, A.W.search; Macrae, J.I.search; Van Aalten, D.M.F.search
Primary citation Structure and Metal-Dependent Mechanism of Peptidoglycan Deacetylase, a Streptococcal Virulence Factor.
PROC.NATL.ACAD.SCI.USAsearch vol:102, pag:15429 (2005) [PubMed ID 16221761 ]search
Keywords CE-4search, CARBOHYDRATE ESTERASEsearch, PEPTIDOGLYCAN DEACETYLASEsearch, METALLOENZYMEsearch, HYDROLASEsearch
Organism Streptococcus pneumoniae R6 171101search(A)
UniProt Peptidoglycan GlcNAc deacetylase (EC 3.5.1.-) Q8DP63search (A)
Solvent A
Polymers
Id Name Type UniProt Residues Observed
A PEPTIDOGLYCAN GLCNAC DEACETYLASE Protein Q8DP63 (Q8DP63_STRR6)search
431 89%
Heterogens
Id Name Ligands
A ACETATE ION ACT search
A ZINC ION ZN search
A DI(HYDROXYETHYL)ETHER PEG search
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