1UBY
STRUCTURE OF FARNESYL PYROPHOSPHATE SYNTHETASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004161 | molecular_function | dimethylallyltranstransferase activity |
| A | 0004337 | molecular_function | (2E,6E)-farnesyl diphosphate synthase activity |
| A | 0004659 | molecular_function | prenyltransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006694 | biological_process | steroid biosynthetic process |
| A | 0006695 | biological_process | cholesterol biosynthetic process |
| A | 0008202 | biological_process | steroid metabolic process |
| A | 0008203 | biological_process | cholesterol metabolic process |
| A | 0008299 | biological_process | isoprenoid biosynthetic process |
| A | 0016126 | biological_process | sterol biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| A | 0033384 | biological_process | geranyl diphosphate biosynthetic process |
| A | 0045337 | biological_process | farnesyl diphosphate biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 402 |
| Chain | Residue |
| A | ASP117 |
| A | ASP121 |
| A | DMA401 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 403 |
| Chain | Residue |
| A | ASP117 |
| A | ASP121 |
| A | GLN185 |
| A | ASP188 |
| A | DMA401 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE DMA A 401 |
| Chain | Residue |
| A | ASP121 |
| A | ARG126 |
| A | LYS214 |
| A | TYR218 |
| A | MG402 |
| A | MG403 |
| A | ASP117 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P14324","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Important for determining product chain length"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1fps |
| Chain | Residue | Details |
| A | ARG126 | |
| A | PHE253 |
| site_id | MCSA1 |
| Number of Residues | 10 |
| Details | M-CSA 253 |
| Chain | Residue | Details |
| A | LYS71 | electrostatic stabiliser |
| A | ASP258 | activator |
| A | ALA112 | steric role |
| A | ASP117 | metal ligand |
| A | ASP121 | metal ligand |
| A | ARG126 | electrostatic stabiliser |
| A | ASP188 | electrostatic stabiliser |
| A | LYS214 | electrostatic stabiliser |
| A | PHE253 | steric role |
| A | ASP257 | metal ligand |
