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 501 |
Chain | Residue |
A | CYS196 |
A | ARG272 |
A | CYS403 |
A | CYS406 |
A | CYS411 |
A | HOH616 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 502 |
Chain | Residue |
A | TRP301 |
A | HOH679 |
B | PRO277 |
B | SER281 |
B | TRP301 |
B | HOH642 |
A | PRO277 |
A | GLN278 |
A | SER281 |
site_id | AC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE CHD A 503 |
Chain | Residue |
A | LEU92 |
A | LEU98 |
A | ARG115 |
A | LYS118 |
A | ILE119 |
A | THR198 |
A | HIS263 |
A | VAL305 |
A | CHD504 |
A | HOH608 |
A | HOH613 |
A | HOH663 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CHD A 504 |
Chain | Residue |
A | LEU98 |
A | MET99 |
A | ARG115 |
A | SER268 |
A | ARG272 |
A | VAL305 |
A | CHD503 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FES B 501 |
Chain | Residue |
B | CYS196 |
B | ARG272 |
B | CYS403 |
B | CYS406 |
B | CYS411 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CHD B 502 |
Chain | Residue |
B | PHE93 |
B | LEU98 |
B | MET99 |
B | ILE111 |
B | ARG114 |
B | ARG115 |
B | CHD504 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CHD B 503 |
Chain | Residue |
B | MET76 |
B | PHE93 |
B | LEU98 |
B | ARG115 |
B | CYS197 |
B | HIS263 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CHD B 504 |
Chain | Residue |
A | LYS106 |
B | ARG114 |
B | CHD502 |
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 | HIS230 | |
B | ASP383 | |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: |
Chain | Residue | Details |
A | CYS196 | |
A | CYS403 | |
A | CYS406 | |
A | CYS411 | |
B | CYS196 | |
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 | 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 | MET76 | |
B | LEU92 | |
B | LEU98 | |
B | ARG164 | |
B | TYR165 | |
B | HIS263 | metal ligand, proton acceptor |
B | ASP340 | |
B | GLU343 | metal ligand, proton acceptor |
B | GLU347 | |