Structural evidence for the partially oxidized dipyrromethene and dipyrromethanone forms of the cofactor of porphobilinogen deaminase: structures of the Bacillus megaterium enzyme at near-atomic resolution

Azim, N.; Deery, E.; Warren, M.J.; Wolfenden, B.A.A.; Erskine, P.; Cooper, J.B.; Coker, A.; Wood, S.P.; Akhtar, M.

doi:10.1107/S139900471303294X

Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

IUCr IT WDC

home archive editors for authors for readers submit subscribe open access

view article

Figure 3
The tertiary structure of B. megaterium PBGD at 1.46 Å resolution showing the oxidized form of the dipyrromethane cofactor covalently attached to Cys241. The domains of the enzyme are numbered 1–3 and the secondary-structure elements are labelled according to the nomenclature of Louie et al. (1992

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 70| Part 3| February 2014| Pages 744-751

doi:10.1107/S139900471303294X

Follow Acta Cryst. D

Search term		doi		Advanced search
Author		volume	page