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spinqualitylabelsall models 1c1m, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

PORCINE ELASTASE UNDER XENON PRESSURE (8 BAR)

Overview

X-ray diffraction is used to study the binding of xenon and krypton to a, variety of crystallised proteins: porcine pancreatic elastase; subtilisin, Carlsberg from Bacillus licheniformis; cutinase from Fusarium solani;, collagenase from Hypoderma lineatum; hen egg lysozyme, the lipoamide, dehydrogenase domain from the outer membrane protein P64k from Neisseria, meningitidis; urate-oxidase from Aspergillus flavus, mosquitocidal, delta-endotoxin CytB from Bacillus thuringiensis and the ligand-binding, domain of the human nuclear retinoid-X receptor RXR-alpha. Under gas, pressures ranging from 8 to 20 bar, xenon is able to bind to discrete, sites in hydrophobic cavities, ligand and substrate binding pockets, and, into the pore of channel-like structures. These xenon complexes can be, used to map hydrophobic sites in proteins, or as heavy-atom derivatives in, the isomorphous replacement method of structure determination.

About this Structure

1C1M is a Single protein structure of sequence from Sus scrofa with CA, SO4 and XE as ligands. Active as Pancreatic elastase, with EC number 3.4.21.36 Full crystallographic information is available from OCA.

Reference

Exploring hydrophobic sites in proteins with xenon or krypton., Prange T, Schiltz M, Pernot L, Colloc'h N, Longhi S, Bourguet W, Fourme R, Proteins. 1998 Jan;30(1):61-73. PMID:9443341

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