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 | 9 |
| Details | binding site for residue GOL A 401 |
| Chain | Residue |
| A | TYR16 |
| A | ALA56 |
| A | THR59 |
| A | GLU60 |
| A | ILE83 |
| A | LEU85 |
| A | PRO90 |
| A | HOH504 |
| A | HOH556 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 402 |
| Chain | Residue |
| A | TYR12 |
| A | HIS182 |
| A | HIS261 |
| A | GLU263 |
| A | PO4409 |
| A | HOH502 |
| A | HOH665 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 403 |
| Chain | Residue |
| A | TYR64 |
| A | ILE83 |
| A | ALA95 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 404 |
| Chain | Residue |
| A | ASP18 |
| A | ILE21 |
| A | ARG43 |
| A | HIS47 |
| A | GLY51 |
| A | LEU52 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 405 |
| Chain | Residue |
| A | TYR12 |
| A | SER120 |
| A | PO4408 |
| A | HOH566 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 406 |
| Chain | Residue |
| A | ILE28 |
| A | HIS30 |
| A | ASP75 |
| A | THR225 |
| A | PO4408 |
| A | HOH505 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 407 |
| Chain | Residue |
| A | LYS33 |
| A | SER35 |
| A | ASN71 |
| A | HOH501 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue PO4 A 408 |
| Chain | Residue |
| A | TYR12 |
| A | ILE28 |
| A | LYS86 |
| A | HIS87 |
| A | GOL405 |
| A | GOL406 |
| A | HOH561 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue PO4 A 409 |
| Chain | Residue |
| A | TYR12 |
| A | HIS182 |
| A | GLU263 |
| A | GOL402 |
| A | HOH505 |
| A | HOH517 |
| A | HOH525 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue K A 410 |
| Chain | Residue |
| A | GLU186 |
| A | GLY231 |
| site_id | AD2 |
| Number of Residues | 1 |
| Details | binding site for residue K A 411 |
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 | ARG45 | |
| A | SER53 | |
| A | TYR124 | |
| A | THR14 | |
| A | ARG29 | |
| Chain | Residue | Details |
| A | HIS182 | |
| A | GLU263 | |
