1od1
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The crystal structure of endothiapepsin complexed with the gem-diol | + | 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. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Coates, L.]] | [[Category: Coates, L.]] | ||
| - | [[Category: Cooper, J | + | [[Category: Cooper, J B.]] |
| - | [[Category: Erskine, P | + | [[Category: Erskine, P T.]] |
| - | [[Category: Gill, R | + | [[Category: Gill, R S.]] |
[[Category: Mall, S.]] | [[Category: Mall, S.]] | ||
| - | [[Category: Wood, S | + | [[Category: Wood, S P.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: acid proteinase]] | [[Category: acid proteinase]] | ||
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[[Category: inhibitor]] | [[Category: inhibitor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:16:15 2008'' |
Revision as of 12:16, 21 February 2008
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ENDOTHIAPEPSIN PD135,040 COMPLEX
Overview
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.
About this Structure
1OD1 is a Protein complex structure of sequences from Cryphonectria parasitica with as ligand. Active as Endothiapepsin, with EC number 3.4.23.22 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 14:16:15 2008
