Cloned (Comment) | Organism |
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Thermoactinomyces vulgaris |
Crystallization (Comment) | Organism |
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in complex with N-benzyloxycarbonyl-L-leucine, at 1.38 A resolution. The structure of the complex is almost identical to that of the free carboxypeptidase T molecule, and a SO42- ion is also localized in the active site. The S1 subsite of carboxypeptidase T is a very conservative structure and negligibly differs from corresponding sites of carboxypeptidase A and carboxypeptidase B in the composition and the 3D structure. The S1 subsite is close to the catalytic zinc ion and to the residues Arg71, Arg147, Arg129, and Glu277 important for catalysis | Thermoactinomyces vulgaris |
Organism | UniProt | Comment | Textmining |
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Thermoactinomyces vulgaris | P29068 | - |
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