2QD5
Structure of wild type human ferrochelatase in complex with a lead-porphyrin compound
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PB A 1101 |
Chain | Residue |
A | ACY801 |
A | ACY803 |
A | PP9901 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PB B 1102 |
Chain | Residue |
B | OXY1001 |
B | PP91105 |
B | ACY1106 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FES A 501 |
Chain | Residue |
A | CYS406 |
A | CYS411 |
A | CYS196 |
A | SER402 |
A | CYS403 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FES B 502 |
Chain | Residue |
B | CYS696 |
B | SER902 |
B | CYS903 |
B | CYS906 |
B | CYS911 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE CHD A 701 |
Chain | Residue |
A | MET99 |
A | ARG115 |
A | PRO266 |
A | SER268 |
A | VAL305 |
A | GLY306 |
A | MET308 |
A | CHD702 |
A | HOH1176 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CHD A 702 |
Chain | Residue |
A | ARG114 |
A | CHD701 |
B | ILE603 |
B | LYS606 |
B | PHE610 |
site_id | AC7 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE CHD B 1103 |
Chain | Residue |
B | LEU601 |
B | PRO766 |
B | SER768 |
B | VAL805 |
B | GLY806 |
B | MET808 |
B | CHD1104 |
B | PP91105 |
B | HOH1108 |
B | HOH1162 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CHD B 1104 |
Chain | Residue |
A | LYS106 |
A | PHE110 |
B | LEU601 |
B | PRO602 |
B | CHD1103 |
site_id | AC9 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE PP9 A 901 |
Chain | Residue |
A | MET76 |
A | PHE93 |
A | LEU98 |
A | ARG115 |
A | ILE119 |
A | SER195 |
A | SER197 |
A | HIS263 |
A | LEU265 |
A | PRO266 |
A | ALA336 |
A | PHE337 |
A | HIS341 |
A | ILE342 |
A | ACY801 |
A | ACY803 |
A | PB1101 |
A | HOH1102 |
A | HOH1160 |
site_id | BC1 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE PP9 B 1105 |
Chain | Residue |
B | MET576 |
B | PHE593 |
B | LEU598 |
B | ARG615 |
B | TYR623 |
B | TYR691 |
B | SER697 |
B | HIS763 |
B | LEU765 |
B | PRO766 |
B | TYR776 |
B | VAL805 |
B | ALA836 |
B | PHE837 |
B | HIS841 |
B | ILE842 |
B | PB1102 |
B | CHD1103 |
B | ACY1106 |
B | HOH1154 |
B | HOH1159 |
site_id | BC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE OXY B 1001 |
Chain | Residue |
B | PB1102 |
site_id | BC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 601 |
Chain | Residue |
A | PRO277 |
A | SER281 |
A | TRP301 |
A | HOH1131 |
B | PRO777 |
B | SER781 |
B | TRP801 |
site_id | BC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ACY A 801 |
Chain | Residue |
A | PP9901 |
A | PB1101 |
A | MET76 |
A | LEU98 |
A | TYR165 |
A | TYR191 |
A | SER197 |
A | THR198 |
site_id | BC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE ACY B 1106 |
Chain | Residue |
B | HIS763 |
B | SER764 |
B | GLN802 |
B | SER803 |
B | LYS804 |
B | TRP810 |
B | PB1102 |
B | PP91105 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ACY A 803 |
Chain | Residue |
A | SER264 |
A | SER303 |
A | LYS304 |
A | TRP310 |
A | PP9901 |
A | PB1101 |
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 | Active site: {"evidences":[{"source":"PubMed","id":"11175906","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
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 | 2 |
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 | 6 |
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 | 2 |
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 | 2 |
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 | 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 |