The structure of endothiapepsin complexed with the gem-diol inhibitor PD-135,040 at 1.37 angstrom
Coates, L., Erskine, P.T., Mall, S., Williams, P.A., Gill, R.S., Wood, S.P. and Cooper, J.B. (2003) The structure of endothiapepsin complexed with the gem-diol inhibitor PD-135,040 at 1.37 angstrom. Acta Crystallographica Section D, Biological Crystallography, 59, (6), 978-981. (doi:10.1107/S0907444903006267).
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The crystal structure of endothiapepsin complexed with the gem-diol inhibitor PD-135,040 has been anisotropically refined to a resolution of 1.37 Å. The structure of this inhibitor complex is in agreement with previous structures of endothiapepsin gem-diol inhibitor complexes that have been used to develop proposed catalytic mechanisms. However, the increase in resolution over previous structures confirms the presence of a number of short hydrogen bonds within the active site that are likely to play an important role in the catalytic mechanism. The presence of low-barrier hydrogen bonds was indicated in a previous one-dimensional H NMR spectrum.
|Subjects:||Q Science > QD Chemistry
Q Science > QH Natural history > QH301 Biology
|Divisions:||University Structure - Pre August 2011 > School of Biological Sciences
|Date Deposited:||06 Aug 2008|
|Last Modified:||12 May 2013 01:19|
|Contributors:||Coates, L. (Author)
Erskine, P.T. (Author)
Mall, S. (Author)
Williams, P.A. (Author)
Gill, R.S. (Author)
Wood, S.P. (Author)
Cooper, J.B. (Author)
|Date:||1 June 2003|
|RDF:||RDF+N-Triples, RDF+N3, RDF+XML, Browse.|
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