1hle | pdb_00001hle
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CRYSTAL STRUCTURE OF CLEAVED EQUINE LEUCOCYTE ELASTASE INHIBITOR DETERMINED AT 1.95 ANGSTROMS RESOLUTION
Overview
The crystal structure of active-site cleaved equine leucocyte elastase, inhibitor, a member of the serpin superfamily, has been solved and refined, to a crystallographic R-factor of 17.6% at 1.95 A resolution. Despite, being an intracellular inhibitor with rather low sequence homology of 30%, to human alpha 1-antichymotrypsin and alpha 1-proteinase inhibitor, the, three-dimensional structures are very similar, with deviations only at the, sites of insertions and few mobile secondary structure elements. The, better resolution in comparison with the structures of other cleaved, serpins allows a more precise description of the so-called R-state of the, serpins.
About this Structure
1HLE is a Protein complex structure of sequences from Equus caballus with CA and ACE as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of cleaved equine leucocyte elastase inhibitor determined at 1.95 A resolution., Baumann U, Bode W, Huber R, Travis J, Potempa J, J Mol Biol. 1992 Aug 20;226(4):1207-18. PMID:1518052
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