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PDBe Entry: 2aut view

Crystal structure of Lys154Asn mutant of mature AphA of S. typhimurium
Summary
Header Hydrolasesearch
Method X-RAY DIFFRACTION
Experiment Resolution: 2.25 Å, R-factor: 15.1%, Free R-factor: 19.7%, Spacegroup: P 21 21 21
Released 05/09/2006, deposition: 29/08/2005, last revision: 24/02/2009
Authors Makde, R.D.search; Gupta, G.D.search; Kumar, V.search
Primary citation Structural and mutational analyses reveal the functional role of active-site Lys-154 and Asp-173 of Salmonella typhimurium AphA protein.
ARCH.BIOCHEM.BIOPHYS.search vol:464, pag:70-79 (2007) [PubMed ID 17570338 ]search
Keywords Class-B bacterial non-specific acid phosphatasesearch, Lys154Asn mutant of mature AphAsearch, metalloenzymesearch, Hydrolasesearch
EC 3.1.3.2 ExPASy BRENDA search (A B C D)
Organism Salmonella enterica subsp. enterica serovar Typhimurium 90371search(A B C D)
UniProt Class B acid phosphatase precursor (EC 3.1.3.2) P58683search (A B C D)
Solvent A, B, C, D
Related entries 1z5g, 1z5u, 1z88
Polymers
Id Name Type UniProt Residues Observed
A, B, C, D AphA Protein P58683 (APHA_SALTY)search
214 98%
Heterogens
Id Name Ligands
A, B, C, D MAGNESIUM ION MG search
D SODIUM ION NA search
D PHOSPHATE ION PO4 search
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