1od1

Endothiapepsin PD135,040 complex

spinqualitylabelsall models 1od1, resolution 1.37Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1od1 is a 1 chain structure with sequence from Cryphonectria parasitica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 0QS, SO4 Related: 1e5o, 1e80, 1e81, 1e82, 1eed, 1ent, 1epl, 1epm, 1epn, 1epo, 1epp, 1epq, 1epr, 1er8, 1gkt, 1gvt, 1gvu, 1gvv, 1gvw, 1gvx, 2er0, 2er6, 2er7, 2er9, 3er3, 3er5, 4ape, 4er1, 4er2, 4er4, 5er1, 5er2 Activity: Endothiapepsin, with EC number 3.4.23.22 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pepsin

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