1a2z
From Proteopedia
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PYRROLIDONE CARBOXYL PEPTIDASE FROM THERMOCOCCUS LITORALIS
Overview
BACKGROUND: Pyrrolidone carboxyl peptidases (pcps) are a group of, exopeptidases responsible for the hydrolysis of N-terminal pyroglutamate, residues from peptides and proteins. The bacterial and archaeal pcps are, members of a conserved family of cysteine proteases. The pcp from the, hyperthermophilic archaeon Thermococcus litoralis is more thermostable, than the bacterial enzymes with which it has up to 40% sequence identity., The pcp activity in archaea and eubacteria is proposed to be involved in, detoxification processes and in nutrient metabolism; eukaryotic, counterparts of the enzyme are involved in the processing of biologically, active peptides. RESULTS: The crystal structure of pcp has been determined, by multiple isomorphous replacement techniques at 1.73 A resolution and, ... [(full description)]
About this Structure
1A2Z is a [Single protein] structure of sequence from [Thermococcus litoralis] with SO4 as [ligand]. Active as [Pyroglutamyl-peptidase I], with EC number [3.4.19.3]. Structure known Active Site: AVE. Full crystallographic information is available from [OCA].
Reference
X-ray structure of pyrrolidone carboxyl peptidase from the hyperthermophilic archaeon Thermococcus litoralis., Singleton M, Isupov M, Littlechild J, Structure. 1999 Mar 15;7(3):237-44. PMID:10368293
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