4KLA
E343D variant of human ferrochelatase
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CHD A 501 |
| Chain | Residue |
| A | MET99 |
| A | ARG115 |
| A | CHD502 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CHD A 502 |
| Chain | Residue |
| A | HOH689 |
| A | HOH702 |
| A | LEU92 |
| A | LEU98 |
| A | LYS118 |
| A | HIS263 |
| A | VAL305 |
| A | CHD501 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 503 |
| Chain | Residue |
| A | PRO277 |
| A | SER281 |
| A | TRP301 |
| A | HOH634 |
| B | PRO277 |
| B | TRP301 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FES A 504 |
| Chain | Residue |
| A | CYS196 |
| A | SER402 |
| A | CYS403 |
| A | CYS406 |
| A | CYS411 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CHD B 501 |
| Chain | Residue |
| B | ARG114 |
| B | ARG115 |
| B | PRO266 |
| B | PP9502 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PP9 B 502 |
| Chain | Residue |
| B | PHE88 |
| B | ARG115 |
| B | TYR123 |
| B | SER197 |
| B | THR198 |
| B | HIS263 |
| B | LEU265 |
| B | PRO266 |
| B | VAL269 |
| B | TYR276 |
| B | HIS341 |
| B | ILE342 |
| B | CHD501 |
| B | HOH602 |
| B | HOH665 |
| B | HOH677 |
| B | HOH682 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FES B 503 |
| Chain | Residue |
| B | CYS196 |
| B | CYS403 |
| B | CYS406 |
| B | 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 | 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 |
