Structural highlights
Function
CARP_CRYPA
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structure of endothiapepsin complexed with the gem-diol inhibitor PD-135,040 has been anisotropically refined to a resolution of 1.37 A. 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.
The structure of endothiapepsin complexed with the gem-diol inhibitor PD-135,040 at 1.37 A.,Coates L, Erskine PT, Mall S, Williams PA, Gill RS, Wood SP, Cooper JB Acta Crystallogr D Biol Crystallogr. 2003 Jun;59(Pt 6):978-81. Epub 2003, May 23. PMID:12777758[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Coates L, Erskine PT, Mall S, Williams PA, Gill RS, Wood SP, Cooper JB. The structure of endothiapepsin complexed with the gem-diol inhibitor PD-135,040 at 1.37 A. Acta Crystallogr D Biol Crystallogr. 2003 Jun;59(Pt 6):978-81. Epub 2003, May 23. PMID:12777758
