2HRE
Structure of human ferrochelatase variant E343K with protoporphyrin IX bound
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 |
| C | 0004325 | molecular_function | ferrochelatase activity |
| C | 0006783 | biological_process | heme biosynthetic process |
| D | 0004325 | molecular_function | ferrochelatase activity |
| D | 0006783 | biological_process | heme biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE PP9 A 601 |
| Chain | Residue |
| A | MET76 |
| A | ILE119 |
| A | TYR123 |
| A | SER130 |
| A | TYR191 |
| A | SER197 |
| A | THR198 |
| A | HIS263 |
| A | PRO266 |
| A | TYR276 |
| A | VAL305 |
| A | GLY77 |
| A | TRP310 |
| A | ALA336 |
| A | HIS341 |
| A | ILE342 |
| A | LYS343 |
| A | GLY78 |
| A | PHE88 |
| A | LEU89 |
| A | LEU92 |
| A | LEU98 |
| A | MET99 |
| A | ARG115 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE PP9 B 602 |
| Chain | Residue |
| B | MET76 |
| B | GLY77 |
| B | GLY78 |
| B | LEU92 |
| B | LEU98 |
| B | MET99 |
| B | ARG115 |
| B | ILE119 |
| B | TYR123 |
| B | SER130 |
| B | ILE132 |
| B | TYR191 |
| B | THR198 |
| B | HIS263 |
| B | PRO266 |
| B | TYR276 |
| B | TRP310 |
| B | ALA336 |
| B | HIS341 |
| B | ILE342 |
| B | LYS343 |
| B | HOH725 |
| B | HOH727 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PP9 B 603 |
| Chain | Residue |
| B | ILE111 |
| B | PRO307 |
| B | MET308 |
| B | CHD701 |
| B | HOH766 |
| D | PRO102 |
| D | PHE110 |
| D | ARG114 |
| D | PP9604 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PP9 D 604 |
| Chain | Residue |
| B | PHE110 |
| B | ARG114 |
| B | PP9603 |
| D | ILE111 |
| D | PRO307 |
| D | MET308 |
| D | CHD702 |
| D | HOH727 |
| D | HOH728 |
| D | HOH729 |
| site_id | AC5 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE PP9 C 605 |
| Chain | Residue |
| C | MET76 |
| C | GLY77 |
| C | GLY78 |
| C | LEU92 |
| C | PHE93 |
| C | LEU98 |
| C | ARG115 |
| C | ILE119 |
| C | TYR123 |
| C | SER130 |
| C | TYR191 |
| C | SER197 |
| C | THR198 |
| C | HIS263 |
| C | PRO266 |
| C | VAL305 |
| C | TRP310 |
| C | ALA336 |
| C | PHE337 |
| C | HIS341 |
| C | ILE342 |
| C | LYS343 |
| site_id | AC6 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE PP9 D 606 |
| Chain | Residue |
| D | SER197 |
| D | THR198 |
| D | HIS263 |
| D | LEU265 |
| D | PRO266 |
| D | TRP310 |
| D | ALA336 |
| D | PHE337 |
| D | HIS341 |
| D | ILE342 |
| D | LYS343 |
| D | MET76 |
| D | GLY77 |
| D | GLY78 |
| D | LEU92 |
| D | PHE93 |
| D | LEU98 |
| D | ARG115 |
| D | ILE119 |
| D | TYR123 |
| D | SER130 |
| D | TYR191 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CHD B 701 |
| Chain | Residue |
| B | LYS118 |
| B | PRO307 |
| B | PP9603 |
| D | HOH719 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CHD D 702 |
| Chain | Residue |
| D | ARG115 |
| D | GLY306 |
| D | PRO307 |
| D | PP9604 |
| D | HOH703 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FES A 501 |
| Chain | Residue |
| A | CYS196 |
| A | SER402 |
| A | CYS403 |
| A | CYS406 |
| A | CYS411 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FES B 502 |
| Chain | Residue |
| B | CYS196 |
| B | ARG272 |
| B | SER402 |
| B | CYS403 |
| B | CYS406 |
| B | CYS411 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FES C 503 |
| Chain | Residue |
| C | CYS196 |
| C | SER402 |
| C | CYS403 |
| C | CYS406 |
| C | CYS411 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FES D 504 |
| Chain | Residue |
| D | CYS196 |
| D | ARG272 |
| D | SER402 |
| D | CYS403 |
| D | CYS406 |
| D | CYS411 |
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 | 8 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"11175906","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17261801","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2HRE","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11175906","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17261801","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1HRK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HRC","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11175906","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1HRK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P22315","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P22315","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1hrk |
| Chain | Residue | Details |
| A | LYS343 | |
| A | HIS263 | |
| A | HIS341 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1hrk |
| Chain | Residue | Details |
| B | LYS343 | |
| B | HIS263 | |
| B | HIS341 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1hrk |
| Chain | Residue | Details |
| C | LYS343 | |
| C | HIS263 | |
| C | HIS341 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1hrk |
| Chain | Residue | Details |
| D | LYS343 | |
| D | HIS263 | |
| D | 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 | HIS263 | metal ligand, proton acceptor |
| A | ASP340 | |
| A | LYS343 | 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 | LYS343 | metal ligand, proton acceptor |
| B | GLU347 |
| site_id | MCSA3 |
| Number of Residues | 9 |
| Details | M-CSA 578 |
| Chain | Residue | Details |
| C | MET76 | |
| C | LEU92 | |
| C | LEU98 | |
| C | ARG164 | |
| C | TYR165 | |
| C | HIS263 | metal ligand, proton acceptor |
| C | ASP340 | |
| C | LYS343 | metal ligand, proton acceptor |
| C | GLU347 |
| site_id | MCSA4 |
| Number of Residues | 9 |
| Details | M-CSA 578 |
| Chain | Residue | Details |
| D | MET76 | |
| D | LEU92 | |
| D | LEU98 | |
| D | ARG164 | |
| D | TYR165 | |
| D | HIS263 | metal ligand, proton acceptor |
| D | ASP340 | |
| D | LYS343 | metal ligand, proton acceptor |
| D | GLU347 |
