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 499 |
| Chain | Residue |
| A | CYS196 |
| A | ARG272 |
| A | CYS403 |
| A | CYS406 |
| A | CYS411 |
| A | HOH516 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FES B 999 |
| Chain | Residue |
| B | CYS406 |
| B | CYS411 |
| B | CYS196 |
| B | ARG272 |
| B | CYS403 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE CHD A 501 |
| Chain | Residue |
| A | MET76 |
| A | LEU92 |
| A | PHE93 |
| A | LEU98 |
| A | MET99 |
| A | SER197 |
| A | LEU265 |
| A | PRO266 |
| A | VAL269 |
| A | VAL305 |
| A | TRP310 |
| A | CHD502 |
| A | HOH616 |
| A | HOH654 |
| A | HOH660 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CHD A 502 |
| Chain | Residue |
| A | MET99 |
| A | ARG114 |
| A | LEU115 |
| A | PRO266 |
| A | VAL305 |
| A | MET308 |
| A | CHD501 |
| A | CHD503 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CHD A 503 |
| Chain | Residue |
| A | CHD502 |
| B | LEU107 |
| B | PHE110 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE CHD B 501 |
| Chain | Residue |
| B | LEU92 |
| B | PHE93 |
| B | LEU98 |
| B | MET99 |
| B | SER197 |
| B | LEU265 |
| B | VAL269 |
| B | VAL305 |
| B | TRP310 |
| B | CHD502 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CHD B 502 |
| Chain | Residue |
| B | ARG114 |
| B | PRO266 |
| B | GLY306 |
| B | MET308 |
| B | CHD501 |
| B | CHD503 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CHD B 503 |
| Chain | Residue |
| A | PHE110 |
| B | LEU101 |
| B | PRO102 |
| B | CHD502 |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | HIS230 | |
| A | ASP383 | |
| B | HIS230 | |
| B | ASP383 | |
| Chain | Residue | Details |
| A | LEU115 | |
| A | TYR123 | |
| A | SER130 | |
| B | LEU115 | |
| 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 | CYS263 | |
| A | HIS341 | |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1hrk |
| Chain | Residue | Details |
| B | GLU343 | |
| B | CYS263 | |
| 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 | CYS263 | 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 | CYS263 | metal ligand, proton acceptor |
| B | ASP340 | |
| B | GLU343 | metal ligand, proton acceptor |
| B | GLU347 | |
