1c3l: Difference between revisions

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|PDB= 1c3l |SIZE=350|CAPTION= <scene name='initialview01'>1c3l</scene>, resolution 2.16&Aring;
|PDB= 1c3l |SIZE=350|CAPTION= <scene name='initialview01'>1c3l</scene>, resolution 2.16&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=XE:XENON'>XE</scene> and <scene name='pdbligand=FMT:FORMIC ACID'>FMT</scene>
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=XE:XENON'>XE</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62]  
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] </span>
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=[[1sbc|1SBC]], [[1bfu|1BFU]], [[1bfk|1BFK]], [[1sca|1SCA]], [[1av7|1AV7]], [[1avt|1AVT]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c3l OCA], [http://www.ebi.ac.uk/pdbsum/1c3l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1c3l RCSB]</span>
}}
}}


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[[Category: Schiltz, M.]]
[[Category: Schiltz, M.]]
[[Category: h, N Colloc.]]
[[Category: h, N Colloc.]]
[[Category: CA]]
[[Category: FMT]]
[[Category: XE]]
[[Category: serine-proteinase]]
[[Category: serine-proteinase]]
[[Category: xenon]]
[[Category: xenon]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:19:25 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:13:49 2008''

Revision as of 16:13, 30 March 2008

File:1c3l.gif


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1c3l, resolution 2.16Å
Ligands: CA, FMT, XE
Activity: Subtilisin, with EC number 3.4.21.62
Related: 1SBC, 1BFU, 1BFK, 1SCA, 1AV7, 1AVT


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



SUBTILISIN-CARLSBERG COMPLEXED WITH XENON (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

1C3L is a Single protein structure of sequence from Bacillus licheniformis. 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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