The oxygenating constituent of 3,6-diketocamphane monooxygenase from the CAM plasmid of Pseudomonas putida: the first crystal structure of a type II Baeyer–Villiger monooxygenase

Isupov, M.N.; Schröder, E.; Gibson, R.P.; Beecher, J.; Donadio, G.; Saneei, V.; Dcunha, S.A.; McGhie, E.J.; Sayer, C.; Davenport, C.F.; Lau, P.C.; Hasegawa, Y.; Iwaki, H.; Kadow, M.; Balke, K.; Bornscheuer, U.T.; Bourenkov, G.; Littlechild, J.A.

doi:10.1107/S1399004715017939

Acta Crystallographica Section D
Acta Crystallographica
Section D BIOLOGICAL CRYSTALLOGRAPHY

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Figure 3
A stereo diagram of the active site of 3,6-DKMO viewed from the solvent region. The cofactor FMN, modelled with an occupancy of 0.6, and neighbouring residues are shown as stick models. The positive OMIT F_o − F_c electron-density map contoured at 3.0σ is shown in green and the negative F_o − F_c map contoured at 3.0σ is shown in red. The OMIT difference electron density was calculated by BUSTER using a structure from which all solvent and cofactor molecules had been removed and the model refined to reduce the bias. The figure was prepared using PyMOL (DeLano, 2002

BIOLOGICAL
CRYSTALLOGRAPHY

ISSN: 1399-0047

Volume 71| Part 11| October 2015| Pages 2344-2353

doi:10.1107/S1399004715017939

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