The structure of endothiapepsin complexed with the gem-diol inhibitor PD-135,040 at 1.37 angstrom
The structure of endothiapepsin complexed with the gem-diol inhibitor PD-135,040 at 1.37 angstrom
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.
978-981
Coates, L.
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Erskine, P.T.
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Mall, S.
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Williams, P.A.
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Gill, R.S.
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Wood, S.P.
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Cooper, J.B.
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1 June 2003
Coates, L.
2be36c11-8cb2-4518-a001-953051aa6a23
Erskine, P.T.
c77b60c5-b80c-4e6a-a103-bf57ecfcbcf6
Mall, S.
343a3062-0630-4e15-8d55-ebb4288f3a8b
Williams, P.A.
18f55b81-ad5c-4db1-892a-9bdcc5092a6b
Gill, R.S.
fbd80a07-b8b8-43ef-aa5c-926cec6e2bbf
Wood, S.P.
430faabf-7f5c-4cf6-9bcc-5955f5e09566
Cooper, J.B.
d9f0f6a8-1260-48fc-aa5c-3dbc650e3ec0
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), .
(doi:10.1107/S0907444903006267).
Abstract
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.
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Published date: 1 June 2003
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Local EPrints ID: 56799
URI: http://eprints.soton.ac.uk/id/eprint/56799
ISSN: 0907-4449
PURE UUID: 42afe8d2-e869-4d08-9139-b0ecb9b6d3e3
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Date deposited: 06 Aug 2008
Last modified: 15 Mar 2024 11:03
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Author:
L. Coates
Author:
P.T. Erskine
Author:
S. Mall
Author:
P.A. Williams
Author:
R.S. Gill
Author:
S.P. Wood
Author:
J.B. Cooper
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