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Figure 2
The anchoring interactions of Asn11 OD2 in wild-type TIM (cyan; PDB entry 1n55; complexed with PGA in grey) by hydrogen bonds from Asn11 OD2 to Trp12 N and Lys13 N. In the wild-type TIM active site Asn11 ND2 functions as an oxyanion-hole donor for the aldehyde substrate (Kursula et al., 2001BB22). In A-TIM (green, PDB entry 2vel; complexed with PGA in yellow) the peptide after Trp12 is flipped, causing a different conformation of the Asn11 side chain. Hydrogen-bonding interactions are highlighted by dotted lines.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 72| Part 6| June 2016| Pages 490-499
doi:10.1107/S2053230X16007548
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