1AEC
CRYSTAL STRUCTURE OF ACTINIDIN-E-64 COMPLEX+
Summary for 1AEC
| Entry DOI | 10.2210/pdb1aec/pdb |
| Descriptor | ACTINIDIN, N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE (3 entities in total) |
| Functional Keywords | hydrolase |
| Biological source | Actinidia chinensis |
| Total number of polymer chains | 1 |
| Total formula weight | 23930.40 |
| Authors | Varughese, K.I. (deposition date: 1992-02-05, release date: 1993-10-31, Last modification date: 2024-10-09) |
| Primary citation | Varughese, K.I.,Su, Y.,Cromwell, D.,Hasnain, S.,Xuong, N.H. Crystal structure of an actinidin-E-64 complex. Biochemistry, 31:5172-5176, 1992 Cited by PubMed Abstract: 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. PubMed: 1606141DOI: 10.1021/bi00137a012 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.86 Å) |
Structure validation
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