1C3L

SUBTILISIN-CARLSBERG COMPLEXED WITH XENON (8 BAR)

Summary for 1C3L

• Entry DOI: 10.2210/pdb1c3l/pdb
• Related: 1AV7 1AVT 1BFK 1BFU 1SBC 1SCA
• Descriptor: SUBTILISIN-CARLSBERG, CALCIUM ION, XENON, ... (5 entities in total)
• Functional Keywords: xenon, serine-proteinase, hydrolase
• Biological source: Bacillus licheniformis
• Cellular location: Secreted: P00780
• Total number of polymer chains: 1
• Total formula weight: 27628.70

Authors

Prange, T.,Schiltz, M.,Pernot, L.,Colloc'h, N.,Longhi, S. (deposition date: 1999-07-28, release date: 1999-08-04, Last modification date: 2023-08-09)

Primary citation

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

PubMed Abstract: 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.

PubMed: 9443341
DOI: 10.1002/(SICI)1097-0134(19980101)30:1<61::AID-PROT6>3.3.CO;2-O

Experimental method

X-RAY DIFFRACTION (2.16 Å)