1bro | pdb_00001bro

BROMOPEROXIDASE A2

spinqualitylabelsall models 1bro, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1bro is a 2 chain structure with sequence from Atcc 10762. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: BPOA2 (ATCC 10762) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [BPOA2_STRAU] May be a chlorinating enzyme involved in 7-chlorotetracycline biosynthesis. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. The metal-ion-free oxidoreductase from Streptomyces aureofaciens has an alpha/beta hydrolase fold.,Hecht HJ, Sobek H, Haag T, Pfeifer O, van Pee KH Nat Struct Biol. 1994 Aug;1(8):532-7. PMID:7664081 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA