Crystallographic characterization of the (R)-selective amine transaminase from Aspergillus fumigatus

Thomsen, M.; Skalden, L.; Palm, G.J.; Höhne, M.; Bornscheuer, U.T.; Hinrichs, W.

doi:10.1107/S1399004714001084

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 3
Comparison of the overall monomer fold between the (R)-selective amine transaminase from A. fumigatus (green), D-amino-acid aminotransferase (PDB entry 3lqs; r.m.s.d. 2.0 Å, cyan) and branched-chain amino-acid aminotransferase (PDB entry 1wrv; r.m.s.d. 1.8 Å, violet) distinctly shows the unique long N-terminal helix found in the (R)-selective amine transaminase. The cofactor PLP is shown as a stick model in yellow.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 70| Part 4| April 2014| Pages 1086-1093

https://doi.org/10.1107/S1399004714001084

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