1HLE

CRYSTAL STRUCTURE OF CLEAVED EQUINE LEUCOCYTE ELASTASE INHIBITOR DETERMINED AT 1.95 ANGSTROMS RESOLUTION

Summary for 1HLE

• Entry DOI: 10.2210/pdb1hle/pdb
• Descriptor: HORSE LEUKOCYTE ELASTASE INHIBITOR, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: hydrolase inhibitor(serine proteinase)
• Biological source: Equus caballus (horse); More
• Cellular location: Cytoplasm : P05619 P05619
• Total number of polymer chains: 2
• Total formula weight: 42636.66

Authors

Baumann, U.,Bode, W.,Huber, R.,Travis, J.,Potempa, J. (deposition date: 1992-04-13, release date: 1994-01-31, Last modification date: 2024-11-13)

Primary citation

Baumann, U.,Bode, W.,Huber, R.,Travis, J.,Potempa, J.
Crystal structure of cleaved equine leucocyte elastase inhibitor determined at 1.95 A resolution.
J.Mol.Biol., 226:1207-1218, 1992

PubMed Abstract: 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.

PubMed: 1518052
DOI: 10.1016/0022-2836(92)91062-T

Experimental method

X-RAY DIFFRACTION (1.95 Å)