1esc

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1esc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1esc OCA], [https://pdbe.org/1esc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1esc RCSB], [https://www.ebi.ac.uk/pdbsum/1esc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1esc ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

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.

A novel variant of the catalytic triad in the Streptomyces scabies esterase.,Wei Y, Schottel JL, Derewenda U, Swenson L, Patkar S, Derewenda ZS Nat Struct Biol. 1995 Mar;2(3):218-23. PMID:7773790<ref>PMID:7773790</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1esc" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Derewenda, U]]

[[Category: Derewenda, Z S]]

[[Category: Patkar, S]]

[[Category: Schottel, J L]]

[[Category: Swenson, L]]

[[Category: Wei, Y]]