While well characterized in animals, bacterial ferrochelatases were discovered much later and seen to differ from animal homologues. Eukaryotic ferrochelatases, typically possess three regions, an N-terminal organelle targeting region that is proteolytically cleaved, a second core region of 330 residues sharing homology with bacterial ferrochelatases and a C-terminal region that contains the dimerization motif as also three of the four cysteine ligands of the 2Fe-2S cluster . It is suggested that mycobacterial ferrochelatases differ from their eukaryotic counterparts in that they are monomers that are not membrane-associated. Rv1485, was hence selected as an ideal test case for whom annotation through our Gefitinib distributor structural pipeline was determined and compared with existing information. Firstly, 1HRK was selected as a template to model Rv1485 . The generated model could be superposed on the template with less than 0.9 Angstrom RMSD . Further, other quality checks were performed to asses the quality of the model using ProCheck, ProQ and ERRAT . Multiple sequence alignments of Rv1485 and homologues from other mycobacteria, Caulobacter crescentus , S. pombe and human ferrochelatases showed a high conservation of residues in the protein core . The alignments show that like the eukaryotic ferrochelatases, such heme synthases also possess a C-terminal region with some of the Cysteine ligands of the 2Fe-2S clusters. The alignments show that S. pombe ferrochelatase contains cysteines analogous to the four cluster-ligating cysteines that are found in animal ferrochelatases. However, C. crescentus ferrochelatase does not possess cysteines in these same position and mycobacterial ferrochelatases possess four-cysteine ligation residues involving C158, C332, C339, and C341 . Examination of the substrate-free and bound forms of the template enzyme show an open active site pocket that is closed through conformation change in the substrate-bound enzyme. Indeed, studies have shown that the active site pocket is closed around the porphyrin macrocycle with a number of active site residues that have reoriented side chains. An important role for a hydrogen bond network involving H263, H341, and E343 has been suggested in the reorganization of active site side chains. Interestingly, a similar network of residues is also seen in the mycobacterial ferrochelatase. PocketDepth and LigsiteCSC predictions, made on the modeled protein identified two pockets that 154447-36-6 overlap with the template pockets harboring the 2Fe�C 2S cluster and the co-crystallized ligand .