4KLC
E343D/F110A Double mutant of human ferrochelatase
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE FES A 501 |
Chain | Residue |
A | CYS196 |
A | ARG272 |
A | SER402 |
A | CYS403 |
A | CYS406 |
A | CYS411 |
A | HOH762 |
site_id | AC2 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE HEM A 502 |
Chain | Residue |
A | PRO79 |
A | LEU92 |
A | PHE93 |
A | LEU98 |
A | TYR123 |
A | SER197 |
A | THR198 |
A | HIS263 |
A | LEU265 |
A | PRO266 |
A | TRP310 |
A | PHE337 |
A | HIS341 |
A | ILE342 |
A | ASP343 |
A | GLY77 |
A | GLY78 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FES B 501 |
Chain | Residue |
B | CYS196 |
B | ARG272 |
B | SER402 |
B | CYS403 |
B | CYS406 |
B | CYS411 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 502 |
Chain | Residue |
A | PRO277 |
A | SER281 |
A | HOH693 |
B | PRO277 |
B | GLN278 |
B | SER281 |
B | LEU299 |
B | TRP301 |
site_id | AC5 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE HEM B 503 |
Chain | Residue |
B | PHE88 |
B | LEU98 |
B | ARG115 |
B | ILE119 |
B | TYR123 |
B | SER197 |
B | THR198 |
B | HIS263 |
B | LEU265 |
B | PRO266 |
B | TYR276 |
B | VAL305 |
B | PHE337 |
B | HIS341 |
B | ILE342 |
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 | 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 | ASP343 | 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 | ASP343 | metal ligand, proton acceptor |
B | GLU347 |