Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004325 | molecular_function | ferrochelatase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006783 | biological_process | heme biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | binding site for residue FEC A 401 |
| Chain | Residue |
| A | TYR12 |
| A | TYR124 |
| A | HIS182 |
| A | GLY223 |
| A | TRP229 |
| A | HIS261 |
| A | LEU262 |
| A | GLU263 |
| A | HOH519 |
| A | HOH536 |
| A | HOH547 |
| A | THR14 |
| A | HOH554 |
| A | HOH569 |
| A | HOH570 |
| A | HOH574 |
| A | TYR24 |
| A | ILE28 |
| A | ARG29 |
| A | LEU42 |
| A | ARG45 |
| A | TYR46 |
| A | SER53 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 402 |
| Chain | Residue |
| A | ASP27 |
| A | LYS86 |
| A | PHE91 |
| A | ARG127 |
| A | HOH509 |
| A | HOH512 |
| A | HOH648 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 403 |
| Chain | Residue |
| A | SER221 |
| A | GLU222 |
| A | ASP267 |
| A | GLU271 |
| A | HOH502 |
| A | HOH507 |
| A | HOH519 |
Functional Information from PROSITE/UniProt
| site_id | PS00435 |
| Number of Residues | 11 |
| Details | PEROXIDASE_1 Peroxidases proximal heme-ligand signature. DTVLIVSAHSL |
| Chain | Residue | Details |
| A | ASP174-LEU184 | |
| site_id | PS00534 |
| Number of Residues | 19 |
| Details | FERROCHELATASE Ferrochelatase signature. LIvSaHSLPekik.QhNDp...Y |
| Chain | Residue | Details |
| A | LEU177-TYR195 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | TYR12 | |
| Chain | Residue | Details |
| A | THR14 | |
| A | ARG29 | |
| A | ARG45 | |
| A | SER53 | |
| A | TYR124 | |
| Chain | Residue | Details |
| A | HIS182 | |
| A | GLU263 | |
