1ESC
THE MOLECULAR MECHANISM OF ENANTIORECOGNITION BY ESTERASES
Summary for 1ESC
| Entry DOI | 10.2210/pdb1esc/pdb |
| Descriptor | ESTERASE (2 entities in total) |
| Functional Keywords | hydrolase (serine esterase) |
| Biological source | Streptomyces scabiei |
| Total number of polymer chains | 1 |
| Total formula weight | 33003.75 |
| Authors | Wei, Y.,Schottel, J.L.,Derewenda, U.,Swenson, L.,Patkar, S.,Derewenda, Z.S. (deposition date: 1994-10-07, release date: 1995-10-15, Last modification date: 2024-10-30) |
| Primary citation | Wei, Y.,Schottel, J.L.,Derewenda, U.,Swenson, L.,Patkar, S.,Derewenda, Z.S. A novel variant of the catalytic triad in the Streptomyces scabies esterase. Nat.Struct.Biol., 2:218-223, 1995 Cited by PubMed Abstract: The crystal structure of a novel esterase from Streptomyces scabies, a causal agent of the potato scab disease, was solved at 2.1 A resolution. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases. The active site contains a dyad of Ser 14 and His 283, closely resembling two of the three components of typical Ser-His-Asp(Glu) triads from other serine hydrolases. Proper orientation of the active site imidazol is maintained by a hydrogen bond between the N delta-H group and a main chain oxygen. Thus, the enzyme constitutes the first known natural variation of the chymotrypsin-like triad in which a carboxylic acid is replaced by a neutral hydrogen-bond acceptor. PubMed: 7773790DOI: 10.1038/nsb0395-218 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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