Figure 1.
Figure 1. a, Omit map of Met-Ala-Ser in the PDF−Ni/MAS
structure contoured at 1 .
Figure prepared with BobScript^25. b, Stereo-view of
superimposed C -traces
of the three crystallographically independent copies of peptide
deformylase in complex with the reaction product Met-Ala-Ser.
The numbers refer to amino acid residues. The transformations
for optimal superposition were determined from equivalent C -atoms
using molecule A as a reference and applied to the Ni^2+ ion
(marked as Ni) and the peptide as well. Molecule complexes A, B,
C are shown in green, magenta, blue, respectively. c, Active
site of PDF−Ni (monomer A) with bound catalytic product
Met-Ala-Ser, ordered water molecules W1, W2 and the Ni^2+ ion.
d, A hypothetical model of PDF with bound substrate
formyl-Met-Ala-Ser.
.
Figure prepared with BobScript^25. b, Stereo-view of
superimposed C 
-traces
of the three crystallographically independent copies of peptide
deformylase in complex with the reaction product Met-Ala-Ser.
The numbers refer to amino acid residues. The transformations
for optimal superposition were determined from equivalent C