1nes: Difference between revisions
No edit summary |
No edit summary |
||
| Line 20: | Line 20: | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1nes ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1nes ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
A single crystal of porcine pancreatic elastase was mounted in a thin-walled capillary and allowed to react with acetyl-Ala-Pro-Ala-paranitroanalide. Diffraction data to 1.65 A resolution were measured and the isomorphous structure was solved from the difference Fourier map. The structure contains two surprises. Two molecules of the product: acetyl-Ala-Pro-Ala molecule are bound in the extended binding site. Both molecules are bound backwards with respect to the established mode of peptide binding. | |||
Structure of the product complex of acetyl-Ala-Pro-Ala with porcine pancreatic elastase at 1.65 A resolution.,Meyer EF Jr, Radhakrishnan R, Cole GM, Presta LG J Mol Biol. 1986 Jun 5;189(3):533-9. PMID:3640831<ref>PMID:3640831</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1nes" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Elastase 3D structures|Elastase 3D structures]] | *[[Elastase 3D structures|Elastase 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 08:32, 5 June 2024
STRUCTURE OF THE PRODUCT COMPLEX OF ACETYL-ALA-PRO-ALA WITH PORCINE PANCREATIC ELASTASE AT 1.65 ANGSTROMS RESOLUTIONSTRUCTURE OF THE PRODUCT COMPLEX OF ACETYL-ALA-PRO-ALA WITH PORCINE PANCREATIC ELASTASE AT 1.65 ANGSTROMS RESOLUTION
Structural highlights
FunctionCELA1_PIG Acts upon elastin. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedA single crystal of porcine pancreatic elastase was mounted in a thin-walled capillary and allowed to react with acetyl-Ala-Pro-Ala-paranitroanalide. Diffraction data to 1.65 A resolution were measured and the isomorphous structure was solved from the difference Fourier map. The structure contains two surprises. Two molecules of the product: acetyl-Ala-Pro-Ala molecule are bound in the extended binding site. Both molecules are bound backwards with respect to the established mode of peptide binding. Structure of the product complex of acetyl-Ala-Pro-Ala with porcine pancreatic elastase at 1.65 A resolution.,Meyer EF Jr, Radhakrishnan R, Cole GM, Presta LG J Mol Biol. 1986 Jun 5;189(3):533-9. PMID:3640831[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
| ||||||||||||||||||