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 | 6 |
| Details | BINDING SITE FOR RESIDUE BCT A 1 |
| Chain | Residue |
| A | MET76 |
| A | LEU98 |
| A | TYR165 |
| A | SER197 |
| A | HEM602 |
| A | HOH646 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BCT B 2 |
| Chain | Residue |
| B | TYR191 |
| B | SER197 |
| B | THR198 |
| B | HEM601 |
| B | HOH636 |
| B | MET76 |
| B | LEU98 |
| B | TYR165 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FES A 424 |
| Chain | Residue |
| A | CYS196 |
| A | SER402 |
| A | CYS403 |
| A | CYS406 |
| A | CYS411 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FES B 424 |
| Chain | Residue |
| B | CYS196 |
| B | ARG272 |
| B | SER402 |
| B | CYS403 |
| B | CYS406 |
| B | CYS411 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE IMD A 425 |
| Chain | Residue |
| A | SER264 |
| A | GLN302 |
| A | SER303 |
| A | HEM602 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE IMD B 425 |
| Chain | Residue |
| B | SER264 |
| B | GLN302 |
| B | SER303 |
| B | TRP310 |
| B | HEM601 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE IMD A 3 |
| Chain | Residue |
| A | PRO277 |
| A | HOH738 |
| A | HOH755 |
| B | PRO277 |
| B | SER281 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CHD B 1 |
| Chain | Residue |
| B | CHD4 |
| B | MET99 |
| B | LEU101 |
| B | ARG115 |
| B | LYS118 |
| B | PRO266 |
| B | VAL305 |
| B | GLY306 |
| B | MET308 |
| B | HEM601 |
| B | HOH632 |
| B | HOH737 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CHD A 2 |
| Chain | Residue |
| A | MET99 |
| A | THR100 |
| A | LEU101 |
| A | ARG114 |
| A | ARG115 |
| A | PRO266 |
| A | SER268 |
| A | VAL305 |
| A | CHD426 |
| A | HEM602 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CHD A 426 |
| Chain | Residue |
| A | CHD2 |
| A | LEU101 |
| A | ARG114 |
| A | HOH748 |
| B | LEU107 |
| B | ALA110 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CHD B 4 |
| Chain | Residue |
| A | LYS106 |
| A | ALA110 |
| B | CHD1 |
| B | LEU101 |
| site_id | BC3 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE HEM A 602 |
| Chain | Residue |
| A | BCT1 |
| A | CHD2 |
| A | MET76 |
| A | PHE93 |
| A | LEU98 |
| A | ARG115 |
| A | ILE119 |
| A | TYR191 |
| A | SER197 |
| A | THR198 |
| A | HIS263 |
| A | LEU265 |
| A | PRO266 |
| A | TYR276 |
| A | VAL305 |
| A | ALA336 |
| A | PHE337 |
| A | HIS341 |
| A | ILE342 |
| A | IMD425 |
| A | HOH623 |
| A | HOH691 |
| A | HOH754 |
| site_id | BC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEM B 601 |
| Chain | Residue |
| B | TYR191 |
| B | SER197 |
| B | HIS263 |
| B | LEU265 |
| B | PRO266 |
| B | VAL305 |
| B | TRP310 |
| B | ALA336 |
| B | HIS341 |
| B | ILE342 |
| B | IMD425 |
| B | HOH674 |
| B | CHD1 |
| B | BCT2 |
| B | MET76 |
| B | PHE93 |
| B | ARG115 |
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 | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1hrk |
| Chain | Residue | Details |
| A | GLU343 | |
| A | HIS263 | |
| A | HIS341 | |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1hrk |
| Chain | Residue | Details |
| B | GLU343 | |
| B | HIS263 | |
| B | HIS341 | |
| 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 | GLU343 | 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 | GLU343 | metal ligand, proton acceptor |
| B | GLU347 | |
