1BRO

BROMOPEROXIDASE A2

Summary for 1BRO

• Entry DOI: 10.2210/pdb1bro/pdb
• Descriptor: BROMOPEROXIDASE A2 (2 entities in total)
• Functional Keywords: antibiotic biosynthesis, oxidoreductase, peroxidase, alpha/beta hydrolase fold, haloperoxidase
• Biological source: Streptomyces aureofaciens
• Total number of polymer chains: 2
• Total formula weight: 60556.84

Authors

Hecht, H.J.,Sobek, H.,Haag, T.,Pfeifer, O.,Van Pee, K.H. (deposition date: 1996-06-01, release date: 1996-12-07, Last modification date: 2024-02-07)

Primary citation

Hecht, H.J.,Sobek, H.,Haag, T.,Pfeifer, O.,van Pee, K.H.
The metal-ion-free oxidoreductase from Streptomyces aureofaciens has an alpha/beta hydrolase fold.
Nat.Struct.Biol., 1:532-537, 1994

PubMed Abstract: 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.

PubMed: 7664081
DOI: 10.1038/nsb0894-532

Experimental method

X-RAY DIFFRACTION (2.05 Å)