In this conformation, Mg2+ alone is bound, and the cation is accessible to the extracellular space for export.
In this conformation, a large part of the protein remains close to natively folded, but a 40 residue region is clearly unfolded.
In this conformation, side chains of neighboring amino acids are directing to other directions.
In this conformation, the arginine residue now performs a dual function like its counterparts in the B. stearothermophilus and E. coli enzymes, of both stabilizing the transition state as well as protecting the phosphoryl groups from solvent exposure.
In this conformation, the FAD and FMN isoalloxazines are in van der Waals contact.
In this conformation, the protein would be ready to accept the substrate.
In this conformation, the side chain is pointed away from both the pyruvoyl cofactor and Ser229.
In this conformation L1 is ideally suited to controllably insert two MnIII ions into a cluster.
In this conformation, Gln294 can form a hydrogen bond with O2 of CDP or UDP.
In this conformation, Thr172 is protected from dephosphorylation because access to protein phosphatases is restricted.
In this conformation, a short H⋅⋅⋅F distance can be measured (see below).
