1aec
From Proteopedia
| Line 5: | Line 5: | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=E64:N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE'>E64</scene> | |LIGAND= <scene name='pdbligand=E64:N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE'>E64</scene> | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Actinidain Actinidain], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.14 3.4.22.14] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Actinidain Actinidain], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.14 3.4.22.14] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1aec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aec OCA], [http://www.ebi.ac.uk/pdbsum/1aec PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1aec RCSB]</span> | ||
}} | }} | ||
| Line 24: | Line 27: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Varughese, K I.]] | [[Category: Varughese, K I.]] | ||
| - | [[Category: E64]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''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 18:38:23 2008'' |
Revision as of 15:38, 30 March 2008
| |||||||
| , resolution 1.86Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Actinidain, with EC number 3.4.22.14 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF ACTINIDIN-E-64 COMPLEX+
Overview
E-64, 1-(L-trans-epoxysuccinylleucylamino)-4-guanidinobutane, is a potent and highly selective irreversible inhibitor of cysteine proteases. The crystal structure of a complex of actinidin and E-64 has been determined at 1.86-A resolution by using the difference Fourier method and refined to an R-factor of 14.5%. The electron density map clearly shows that the C2 atom of the E-64 epoxide ring is covalently bonded to the S atom of the active-site cysteine 25. The charged carboxyl group of E-64 forms four H-bonds with the protein and thus may play an important role in favorably positioning the inhibitor molecule for nucleophilic attack by the active-site thiolate anion. The interaction features between E-64 and actinidin are very similar to those seen in the papain-E-64 complex; however, the amino-4-guanidinobutane group orients differently. The crystals of the actinidin-E-64 complex diffracted much better than the papain-E-64 complex, and consequently the present study provides more precise geometrical information on the binding of the inhibitor. Moreover, this study provides yet another confirmation that the binding of E-64 is at the S subsites and not at the S' subsites as has been previously proposed. The original actinidin structure has been revised using the new cDNA sequence information.
About this Structure
1AEC is a Single protein structure of sequence from Actinidia chinensis. Full crystallographic information is available from OCA.
Reference
Crystal structure of an actinidin-E-64 complex., Varughese KI, Su Y, Cromwell D, Hasnain S, Xuong NH, Biochemistry. 1992 Jun 9;31(22):5172-6. PMID:1606141
Page seeded by OCA on Sun Mar 30 18:38:23 2008
