The crystal structure of the bromoperoxidase A2 from Streptomyces aureofaciens (ATCC 10762) has been determined by isomorphous replacement and refined to 2.05 A resolution with an R-value of 18.4%. The enzyme catalyzes the bromination of organic compounds in the presence of bromide and peroxide. The structure confirms the absence of cofactors such as metal ions or haem groups and shows the general topology of the alpha/beta hydrolase fold. The active centre is at the end of a deep pocket and includes a catalytic triad of Ser 98, Asp 228 and His 257. The active centre is connected by a narrow tunnel to a second pocket on the enzyme surface.
        
Representative scheme of Haloperoxidase structure and an image from PDBsum server
Databases
PDB-Sum
1BRO Previously Class, Architecture, Topology and Homologous superfamily - PDB-Sum server
FSSP
1BROFold classification based on Structure-Structure alignment of Proteins - FSSP server