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PDBe Entry: 2c1i view

STRUCTURE OF STREPTOCOCCUS PNEMONIAE PEPTIDOGLYCAN DEACETYLASE (SPPGDA) D 275 N MUTANT.
Summary
Header HYDROLASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 1.35 Å, R-factor: 18.9%, Free R-factor: 22.5%, Spacegroup: P 21 21 21
Released 20/09/2005, deposition: 15/09/2005, 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, D275N MUTANTsearch, HYDROLASEsearch
Organism Streptococcus pneumoniae R6 171101search(A)
UniProt Peptidoglycan GlcNAc deacetylase (EC 3.5.1.-) Q8DP63search (A)
Solvent A
Related entries 2c1g
Polymers
Id Name Type UniProt Residues Observed
A PEPTIDOGLYCAN GLCNAC DEACETYLASE Protein Q8DP63 (Q8DP63_STRR6)search
431 88%
Heterogens
Id Name Ligands
A 2-(N-MORPHOLINO)-ETHANESULFONIC ACID MES search
A ZINC ION ZN search
A SULFATE ION SO4 search
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