4N7B
Structure of the E-1-hydroxy-2-methyl-but-2-enyl-4-diphosphate reductase from Plasmodium falciparum
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008299 | biological_process | isoprenoid biosynthetic process |
| A | 0010322 | biological_process | regulation of isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019288 | biological_process | isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway |
| A | 0020011 | cellular_component | apicoplast |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050992 | biological_process | dimethylallyl diphosphate biosynthetic process |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| A | 0051745 | molecular_function | 4-hydroxy-3-methylbut-2-enyl diphosphate reductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE F3S A 401 |
| Chain | Residue |
| A | CYS14 |
| A | CYS98 |
| A | THR166 |
| A | CYS196 |
| A | HOH538 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A 402 |
| Chain | Residue |
| A | SER224 |
| A | SER225 |
| A | ASN226 |
| A | HOH505 |
| A | HOH506 |
| A | HOH648 |
| A | HIS43 |
| A | HIS76 |
| A | HIS126 |
| A | THR167 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 403 |
| Chain | Residue |
| A | ARG237 |
| A | HOH568 |
| A | HOH587 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 404 |
| Chain | Residue |
| A | PHE13 |
| A | GLU271 |
| A | HOH617 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE NA A 405 |
| Chain | Residue |
| A | TYR107 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA A 406 |
| Chain | Residue |
| A | ALA136 |
| A | PRO137 |
| A | HIS138 |
Functional Information from PROSITE/UniProt
| site_id | PS00092 |
| Number of Residues | 7 |
| Details | N6_MTASE N-6 Adenine-specific DNA methylases signature. LLTNPPF |
| Chain | Residue | Details |
| A | LEU280-PHE286 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P62623","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24188825","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4N7B","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P62623","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
