Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004325 | molecular_function | ferrochelatase activity |
| A | 0006783 | biological_process | heme biosynthetic process |
| B | 0004325 | molecular_function | ferrochelatase activity |
| B | 0006783 | biological_process | heme biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES A 501 |
| Chain | Residue |
| A | CYS196 |
| A | ARG272 |
| A | SER402 |
| A | CYS403 |
| A | CYS406 |
| A | CYS411 |
| A | HOH762 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEM A 502 |
| Chain | Residue |
| A | PRO79 |
| A | LEU92 |
| A | PHE93 |
| A | LEU98 |
| A | TYR123 |
| A | SER197 |
| A | THR198 |
| A | HIS263 |
| A | LEU265 |
| A | PRO266 |
| A | TRP310 |
| A | PHE337 |
| A | HIS341 |
| A | ILE342 |
| A | ASP343 |
| A | GLY77 |
| A | GLY78 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FES B 501 |
| Chain | Residue |
| B | CYS196 |
| B | ARG272 |
| B | SER402 |
| B | CYS403 |
| B | CYS406 |
| B | CYS411 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 502 |
| Chain | Residue |
| A | PRO277 |
| A | SER281 |
| A | HOH693 |
| B | PRO277 |
| B | GLN278 |
| B | SER281 |
| B | LEU299 |
| B | TRP301 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE HEM B 503 |
| Chain | Residue |
| B | PHE88 |
| B | LEU98 |
| B | ARG115 |
| B | ILE119 |
| B | TYR123 |
| B | SER197 |
| B | THR198 |
| B | HIS263 |
| B | LEU265 |
| B | PRO266 |
| B | TYR276 |
| B | VAL305 |
| B | PHE337 |
| B | HIS341 |
| B | ILE342 |
Functional Information from PROSITE/UniProt
| site_id | PS00534 |
| Number of Residues | 19 |
| Details | FERROCHELATASE Ferrochelatase signature. ILfSaHSLPmsvv.NrGDp...Y |
| Chain | Residue | Details |
| A | ILE258-TYR276 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | HIS230 | |
| A | ASP383 | |
| B | HIS230 | |
| B | ASP383 | |
| Chain | Residue | Details |
| A | ARG115 | |
| A | TYR123 | |
| A | SER130 | |
| B | ARG115 | |
| B | TYR123 | |
| B | SER130 | |
| Chain | Residue | Details |
| A | CYS196 | |
| B | CYS196 | |
| Chain | Residue | Details |
| A | CYS403 | |
| A | CYS406 | |
| A | CYS411 | |
| B | CYS403 | |
| B | CYS406 | |
| B | CYS411 | |
| Chain | Residue | Details |
| A | LYS138 | |
| B | LYS138 | |
| Chain | Residue | Details |
| A | LYS415 | |
| B | LYS415 | |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 9 |
| Details | M-CSA 578 |
| Chain | Residue | Details |
| A | MET76 | |
| A | LEU92 | |
| A | LEU98 | |
| A | ARG164 | |
| A | TYR165 | |
| A | HIS263 | metal ligand, proton acceptor |
| A | ASP340 | |
| A | ASP343 | metal ligand, proton acceptor |
| A | GLU347 | |
| site_id | MCSA2 |
| Number of Residues | 9 |
| Details | M-CSA 578 |
| Chain | Residue | Details |
| B | MET76 | |
| B | LEU92 | |
| B | LEU98 | |
| B | ARG164 | |
| B | TYR165 | |
| B | HIS263 | metal ligand, proton acceptor |
| B | ASP340 | |
| B | ASP343 | metal ligand, proton acceptor |
| B | GLU347 | |
