This target is predicted to be act as formyltetrahydrofolate deformylases, which are not known to require ions. So I would discard contacts from metals or other ions. according to CSA data, the catalytic site would include Asn192, His194, Thr221 and Asp230. Our data are not enough for a reliable ligand binding site prediction, because they come from a few complexes bound to valid but not relevant ligands. I have used the SAS service at EBI to align the target sequence to some of the structures with adopting the same fold - CATH code - and involved only in the same reaction - EC Using EC2PDB I collected these PDB codes: 1c2t, 1cde, 1c3e, 1gar, 1men, 1rby and 1zly, which are bound to molecules higly similar or identical to the natural substartes. These ligands are GAR - the enzyme reactant - DZF - very similar to the enzyme product - and NHR/NHS - similar to the enzyme substarte.\\

Residues matching amino acids contacting GAR: Arg173, Tyr174, Met175, Ile193, His194, His195, Arg256, Glu259\\
Consensus of the contacts from DZF, NHS and NHR: Arg150, Tyr174, Met175, Gln176, Ile177, Leu178, Ser183, Asn192, His194, Ala204, Val225, Thr226, Ser227, Ala228, Leu229, Asp230\\

TARGET T0613\\
AUTHOR 7656-5034-1890\\
REMARK Sequence consensus of contacts between homologous structures and ligands\\
METHOD pGenTHREADER and PDBSum and CSA data mining.\\
Binding site: 150, 173, 174, 175, 176, 177, 178, 183, 192, 193, 194, 195, 204, 221, 225, 226, 227, 228, 229, 230, 256, 259\\