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Alexander W. Schüttelkopf
Researcher at University of Dundee
Publications - 29
Citations - 6544
Alexander W. Schüttelkopf is an academic researcher from University of Dundee. The author has contributed to research in topics: Enzyme & Active site. The author has an hindex of 21, co-authored 28 publications receiving 5799 citations. Previous affiliations of Alexander W. Schüttelkopf include University of British Columbia.
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PRODRG: a tool for high-throughput crystallography of protein–ligand complexes
TL;DR: The small-molecule topology generator PRODRG is described, which takes input from existing coordinates or various two-dimensional formats and automatically generates coordinates and molecular topologies suitable for X-ray refinement of protein-ligand complexes.
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ALINE: a WYSIWYG protein‐sequence alignment editor for publication‐quality alignments
TL;DR: ALINE is a portable interactive graphical sequence-alignment editor implemented in Perl/Tk which produces publication-quality sequence-Alignment figures where "what you see is what you get".
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Structure and metal-dependent mechanism of peptidoglycan deacetylase, a streptococcal virulence factor
TL;DR: The data described here show that SpPgdA and the other family 4 carbohydrate esterases are metalloenzymes and present a step toward identification of mechanism-based inhibitors for this important class of enzymes.
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Structure and mechanism of chitin deacetylase from the fungal pathogen Colletotrichum lindemuthianum.
D.E. Blair,Omid Hekmat,Alexander W. Schüttelkopf,Binesh Shrestha,Ken Tokuyasu,Stephen G. Withers,Daan M. F. van Aalten +6 more
TL;DR: The data presented here indicate that ClCDA possesses a highly conserved substrate-binding groove, with subtle alterations that influence substrate specificity and subsite affinity, and shows that the hexahistidine purification tag appears to form a tight interaction with the active site groove.
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O-GlcNAc transferase invokes nucleotide sugar pyrophosphate participation in catalysis.
Marianne Schimpl,Xiaowei Zheng,Vladimir S. Borodkin,D.E. Blair,Andrew T. Ferenbach,Alexander W. Schüttelkopf,Iva Navratilova,Tonia Aristotelous,Osama Albarbarawi,David A. Robinson,Megan A. Macnaughtan,Daan M. F. van Aalten +11 more
TL;DR: This work defines how human O-GlcNAc transferase recognizes the sugar donor and acceptor peptide and employs a novel catalytic mechanism of glycosyl transfer, involving the sugar donors α-phosphate as the catalytic base, as well as an essential lysine.