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 | 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 | HIS841 | |
B | HIS763 | |
B | GLU843 | |
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 | |