1RQI
Active Conformation of Farnesyl Pyrophosphate Synthase Bound to Isopentyl Pyrophosphate and Dimethylallyl S-Thiolodiphosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004161 | molecular_function | dimethylallyltranstransferase activity |
| A | 0004337 | molecular_function | geranyltranstransferase activity |
| A | 0004659 | molecular_function | prenyltransferase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008299 | biological_process | isoprenoid biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0033384 | biological_process | geranyl diphosphate biosynthetic process |
| A | 0045337 | biological_process | farnesyl diphosphate biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004161 | molecular_function | dimethylallyltranstransferase activity |
| B | 0004337 | molecular_function | geranyltranstransferase activity |
| B | 0004659 | molecular_function | prenyltransferase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0008299 | biological_process | isoprenoid biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0033384 | biological_process | geranyl diphosphate biosynthetic process |
| B | 0045337 | biological_process | farnesyl diphosphate biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 600 |
| Chain | Residue |
| B | ASP244 |
| B | ASP248 |
| B | DST400 |
| B | HOH700 |
| B | HOH701 |
| B | HOH741 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG B 601 |
| Chain | Residue |
| B | MG602 |
| B | HOH704 |
| B | HOH705 |
| B | HOH862 |
| B | ASP105 |
| B | ASP111 |
| B | DST400 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 602 |
| Chain | Residue |
| B | ASP105 |
| B | ASP111 |
| B | DST400 |
| B | MG601 |
| B | HOH702 |
| B | HOH703 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 603 |
| Chain | Residue |
| A | ASP244 |
| A | DST401 |
| A | HOH717 |
| A | HOH718 |
| A | HOH734 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 604 |
| Chain | Residue |
| A | ASP105 |
| A | ASP111 |
| A | DST401 |
| A | MG605 |
| A | HOH721 |
| A | HOH722 |
| A | HOH738 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 605 |
| Chain | Residue |
| A | ASP105 |
| A | ASP111 |
| A | ASP113 |
| A | DST401 |
| A | MG604 |
| A | HOH719 |
| A | HOH720 |
| site_id | AC7 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE DST B 400 |
| Chain | Residue |
| B | SER101 |
| B | ASP105 |
| B | ASP111 |
| B | ARG116 |
| B | MET175 |
| B | GLN179 |
| B | LYS202 |
| B | ASP244 |
| B | LYS258 |
| B | IPR500 |
| B | MG600 |
| B | MG601 |
| B | MG602 |
| B | HOH700 |
| B | HOH701 |
| B | HOH702 |
| B | HOH704 |
| site_id | AC8 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE DST A 401 |
| Chain | Residue |
| A | SER101 |
| A | LEU102 |
| A | ASP105 |
| A | ASP111 |
| A | ARG116 |
| A | MET175 |
| A | GLN179 |
| A | LYS202 |
| A | ASP244 |
| A | LYS258 |
| A | IPR501 |
| A | MG603 |
| A | MG604 |
| A | MG605 |
| A | HOH717 |
| A | HOH718 |
| A | HOH719 |
| A | HOH720 |
| A | HOH721 |
| A | HOH734 |
| A | HOH738 |
| A | HOH835 |
| site_id | AC9 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE IPR B 500 |
| Chain | Residue |
| B | GLY65 |
| B | LYS66 |
| B | ARG69 |
| B | HIS98 |
| B | LEU102 |
| B | ARG117 |
| B | PHE240 |
| B | GLN241 |
| B | ASP244 |
| B | DST400 |
| B | HOH706 |
| B | HOH707 |
| B | HOH710 |
| B | HOH711 |
| B | HOH712 |
| B | HOH713 |
| site_id | BC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE IPR A 501 |
| Chain | Residue |
| A | PHE240 |
| A | GLN241 |
| A | ASP244 |
| A | DST401 |
| A | HOH723 |
| A | HOH724 |
| A | HOH727 |
| A | HOH728 |
| A | HOH729 |
| A | HOH730 |
| A | GLY65 |
| A | LYS66 |
| A | ARG69 |
| A | HIS98 |
| A | ARG117 |
| A | THR203 |
| site_id | BC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE DPO A 606 |
| Chain | Residue |
| A | GLN27 |
| A | ALA30 |
| A | CYS31 |
| A | GLN34 |
| A | PHE71 |
| A | TYR74 |
| A | ALA75 |
| A | HIS78 |
| A | HOH844 |
| A | HOH872 |
| B | HIS189 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:14672944 |
| Chain | Residue | Details |
| A | LYS66 | |
| B | ASP105 | |
| B | ASP111 | |
| B | ARG117 | |
| A | ARG69 | |
| A | HIS98 | |
| A | ASP105 | |
| A | ASP111 | |
| A | ARG117 | |
| B | LYS66 | |
| B | ARG69 | |
| B | HIS98 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ARG116 | |
| B | LYS258 | |
| A | LYS202 | |
| A | THR203 | |
| A | GLN241 | |
| A | LYS258 | |
| B | ARG116 | |
| B | LYS202 | |
| B | THR203 | |
| B | GLN241 |
