Literature summary for 3.1.1.84 extracted from

Larsen, N.A.; Turner, J.M.; Stevens, J.; Rosser, S.J.; Basran, A.; Lerner, R.A.; Bruce, N.C.; Wilson, I.A.
Crystal structure of a bacterial cocaine esterase (2002), Nat. Struct. Biol., 9, 17-21.

Application

Application	Comment	Organism
medicine	because of the high catalytic proficiency of cocE, it is an attractive candidate for novel protein-based therapies for cocaine overdose	Rhodococcus sp.

Crystallization (Commentary)

Crystallization (Comment)	Organism
te crystal structure of cocE, solved by multiple anomalous dispersion methods, reveals that cocE is a serine esterase composed of three domains: (1.) a canonical alpha/beta hydrolase fold (2.) an alpha-helical domain that caps the active site and (3.) a jelly-roll-like beta-domain that interacts extensively with the other two domains. The active site is identified within the interface of all three domains by analysis of the crystal structures of transition state analog adduct and product complexes, which are refined at 1.58 A and 1.63 A resolution, respectively	Rhodococcus sp.

Crystallization (Comment)

Organism

te crystal structure of cocE, solved by multiple anomalous dispersion methods, reveals that cocE is a serine esterase composed of three domains: (1.) a canonical alpha/beta hydrolase fold (2.) an alpha-helical domain that caps the active site and (3.) a jelly-roll-like beta-domain that interacts extensively with the other two domains. The active site is identified within the interface of all three domains by analysis of the crystal structures of transition state analog adduct and product complexes, which are refined at 1.58 A and 1.63 A resolution, respectively

Rhodococcus sp.

Organism

Organism	UniProt	Comment	Textmining
Rhodococcus sp.	Q9L9D7	-	-

Synonyms

Synonyms	Comment	Organism
cocE	-	Rhodococcus sp.

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Release 2023.1 (January 2023)