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 FES A 601 |
| Chain | Residue |
| A | CYS196 |
| A | ARG272 |
| A | SER402 |
| A | CYS403 |
| A | CYS406 |
| A | CYS411 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FES B 924 |
| Chain | Residue |
| B | CYS903 |
| B | CYS906 |
| B | CYS911 |
| B | CYS696 |
| B | ARG772 |
| B | SER902 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEM B 925 |
| Chain | Residue |
| B | CHD504 |
| B | PHE588 |
| B | LEU589 |
| B | ARG615 |
| B | ILE619 |
| B | GLN622 |
| B | TYR623 |
| B | TYR691 |
| B | SER697 |
| B | THR698 |
| B | HIS763 |
| B | LEU765 |
| B | PRO766 |
| B | HIS841 |
| B | ILE842 |
| B | GLU843 |
| B | HOH1000 |
| B | HOH1055 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE CHD A 501 |
| Chain | Residue |
| A | MET76 |
| A | LEU92 |
| A | LEU98 |
| A | ARG115 |
| A | LYS118 |
| A | ILE119 |
| A | HIS263 |
| A | VAL305 |
| A | HOH791 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CHD A 502 |
| Chain | Residue |
| A | PHE93 |
| A | MET99 |
| A | ARG115 |
| A | SER268 |
| A | VAL305 |
| A | GLY306 |
| A | MET308 |
| A | TRP310 |
| A | CHD503 |
| A | HOH626 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CHD A 503 |
| Chain | Residue |
| A | THR100 |
| A | LEU101 |
| A | CHD502 |
| B | ILE603 |
| B | LEU607 |
| B | PHE610 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CHD B 504 |
| Chain | Residue |
| B | CHD505 |
| B | ARG615 |
| B | PRO766 |
| B | HEM925 |
| B | HOH1101 |
| B | HOH1113 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CHD B 505 |
| Chain | Residue |
| A | LYS106 |
| A | PHE110 |
| B | CHD504 |
| B | LEU601 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 506 |
| Chain | Residue |
| A | PRO277 |
| A | SER281 |
| A | TRP301 |
| B | PRO777 |
| B | SER781 |
| B | TRP801 |
| B | HOH993 |
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
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: |
| Chain | Residue | Details |
| A | HIS230 | |
| A | ASP383 | |
| B | HIS730 | |
| B | ASP883 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | CYS196 | |
| A | CYS403 | |
| A | CYS406 | |
| A | CYS411 | |
| B | CYS696 | |
| B | CYS903 | |
| B | CYS906 | |
| B | CYS911 | |
| Chain | Residue | Details |
| A | LYS138 | |
| B | LYS638 | |
| Chain | Residue | Details |
| A | LYS415 | |
| B | LYS915 | |
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 | GLU343 | metal ligand, proton acceptor |
| A | GLU347 | |
| site_id | MCSA2 |
| Number of Residues | 9 |
| Details | M-CSA 578 |
| Chain | Residue | Details |
| B | MET576 | |
| B | LEU592 | |
| B | LEU598 | |
| B | ARG664 | |
| B | TYR665 | |
| B | HIS763 | metal ligand, proton acceptor |
| B | ASP840 | |
| B | GLU843 | metal ligand, proton acceptor |
| B | GLU847 | |
