Structural studies of substrate and product complexes of 5-aminolaevulinic acid dehydratase from humans, Escherichia coli and the hyperthermophile Pyrobaculum calidifontis

Mills-Davies, N.; Butler, D.; Norton, E.; Thompson, D.; Sarwar, M.; Guo, J.; Gill, R.; Azim, N.; Coker, A.; Wood, S.P.; Erskine, P.T.; Coates, L.; Cooper, J.B.; Rashid, N.; Akhtar, M.; Shoolingin-Jordan, P.M.

doi:10.1107/S2059798316019525

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 7
The structure of PBG bound to E. coli ALAD. The refined 2F_o − F_c electron density for the PBG and the active-site zinc ion (grey) is shown as blue lines contoured at 1.0 r.m.s.. The main interacting residues, including the Schiff-base lysines in the foreground, are labelled and hydrogen bonds are indicated by dotted lines.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 73| Part 1| January 2017| Pages 9-21

https://doi.org/10.1107/S2059798316019525

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