1elg: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 1elg |SIZE=350|CAPTION= <scene name='initialview01'>1elg</scene>, resolution 1.65Å | |PDB= 1elg |SIZE=350|CAPTION= <scene name='initialview01'>1elg</scene>, resolution 1.65Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=BAA:(TERT-BUTYLOXYCARBONYL)-ALANYL-ALANYL-AMINE'>BAA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Pancreatic_elastase Pancreatic elastase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.36 3.4.21.36] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Pancreatic_elastase Pancreatic elastase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.36 3.4.21.36] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1elg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1elg OCA], [http://www.ebi.ac.uk/pdbsum/1elg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1elg RCSB]</span> | |||
}} | }} | ||
| Line 28: | Line 31: | ||
[[Category: Ringe, D.]] | [[Category: Ringe, D.]] | ||
[[Category: Steinmetz, A C.U.]] | [[Category: Steinmetz, A C.U.]] | ||
[[Category: complex (hydrolase/inhibitor)]] | [[Category: complex (hydrolase/inhibitor)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:04:55 2008'' | ||
Revision as of 17:05, 30 March 2008
| |||||||||||||
| 1elg, resolution 1.65Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | BAA, CA | ||||||||||||
| Activity: | Pancreatic elastase, with EC number 3.4.21.36 | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
NATURE OF THE INACTIVATION OF ELASTASE BY N-PEPTIDYL-O-AROYL HYDROXYLAMINE AS A FUNCTION OF PH
Overview
The mechanism of inactivation of porcine pancreatic elastase (PPE) by N-peptidyl-O-aroylhydroxylamine was studied by X-ray crystallography. The inactivator forms a stable complex with the enzyme by means of a covalent attachment to the active site Ser 203(195) O gamma. The nature of the complex is, however, different depending on the pH at which the inactivation reaction occurs. At pH 5, the complex formed is a hydroxylamine derivative of Ser 203(195) in which the O gamma of serine is the oxygen of the hydroxylamine derivative. At pH 7.5, the complex formed is a carbamate derivative at Ser 203(195) O gamma. In both types of complexes, the inactivator binds in the S' subsites of the enzyme instead of forming the usual antiparallel beta-sheet with the S subsites. The implication for the mechanism of inactivation at different pHs is discussed.
About this Structure
1ELG is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
Reference
Nature of the inactivation of elastase by N-peptidyl-O-aroyl hydroxylamine as a function of pH., Ding X, Rasmussen BF, Demuth HU, Ringe D, Steinmetz AC, Biochemistry. 1995 Jun 13;34(23):7749-56. PMID:7779821
Page seeded by OCA on Sun Mar 30 20:04:55 2008
