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. 2002 Apr;11(4):903–911. doi: 10.1110/ps.4260102

Fig. 2.

Fig. 2.

SWISS-MODEL of T. maritima (purple) on E. coli (elementally colored [top] or blue [bottom]) produced using the sequence alignment generated for Fig. 1 ▶ and the ED9A E. coli AP coordinates (Stec et al. 2000). (Top) T. maritima and E. coli AP active site overlay showing metal-binding residues highlighted in Fig. 1 ▶. The two zinc ions (blue) and magnesium (cyan) are from the E. coli AP coordinates (Stec et al. 2000). Green dotted lines indicate the salt bridge between E. coli AP residues D153 and K328 and the residue-metal interactions; water-ligand interactions to the magnesium have been eliminated for clarity. (Bottom) Monomeric model of T. maritima AP on E. coli AP. The putative signal sequence has been eliminated from the T. maritima protein as predicted by SignalP and the sequence alignment as stated in the text. The termini and differing regions are highlighted with E. coli (EC) or T. maritima (TM) numbering. T. maritima AP is numbered from the first amino acid including the putative signal sequence.