This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1elf
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1elf |SIZE=350|CAPTION= <scene name='initialview01'>1elf</scene>, resolution 1.7Å | |PDB= 1elf |SIZE=350|CAPTION= <scene name='initialview01'>1elf</scene>, resolution 1.7Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=BAF:(TERT-BUTYLOXYCARBONYL)-ALANYL-AMINO+ETHYL-FORMAMIDE'>BAF</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1elf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1elf OCA], [http://www.ebi.ac.uk/pdbsum/1elf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1elf RCSB]</span> | ||
}} | }} | ||
| Line 28: | Line 31: | ||
[[Category: Ringe, D.]] | [[Category: Ringe, D.]] | ||
[[Category: Steinmetz, A C.U.]] | [[Category: Steinmetz, A C.U.]] | ||
| - | [[Category: BAF]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: SO4]] | ||
[[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 20:04:56 2008'' |
Revision as of 17:04, 30 March 2008
| |||||||
| , resolution 1.7Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| 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
1ELF 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 20:04:56 2008
