1RQJ
Active Conformation of Farnesyl Pyrophosphate Synthase Bound to Isopentyl Pyrophosphate and Risedronate
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 904 |
| Chain | Residue |
| B | ASP244 |
| B | ASP248 |
| B | RIS903 |
| B | HOH933 |
| B | HOH999 |
| B | HOH1000 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG B 905 |
| Chain | Residue |
| B | MG906 |
| B | HOH913 |
| B | HOH1002 |
| B | HOH1003 |
| B | ASP105 |
| B | ASP111 |
| B | RIS903 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 906 |
| Chain | Residue |
| B | ASP105 |
| B | ASP111 |
| B | RIS903 |
| B | MG905 |
| B | HOH945 |
| B | HOH1001 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 907 |
| Chain | Residue |
| A | ASP105 |
| A | ASP111 |
| A | RIS901 |
| A | MG909 |
| A | HOH933 |
| A | HOH945 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 908 |
| Chain | Residue |
| A | ASP244 |
| A | RIS901 |
| A | HOH918 |
| A | HOH1031 |
| A | HOH1032 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG A 909 |
| Chain | Residue |
| A | ASP105 |
| A | ASP111 |
| A | RIS901 |
| A | MG907 |
| A | HOH922 |
| A | HOH926 |
| A | HOH1034 |
| site_id | AC7 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE IPE A 900 |
| Chain | Residue |
| A | GLY65 |
| A | LYS66 |
| A | ARG69 |
| A | HIS98 |
| A | ARG117 |
| A | THR203 |
| A | PHE240 |
| A | GLN241 |
| A | RIS901 |
| A | HOH912 |
| A | HOH913 |
| A | HOH917 |
| A | HOH919 |
| A | HOH973 |
| A | HOH997 |
| site_id | AC8 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE RIS A 901 |
| Chain | Residue |
| A | ASP105 |
| A | ASP111 |
| A | ARG116 |
| A | GLN179 |
| A | LYS202 |
| A | THR203 |
| A | GLN241 |
| A | ASP244 |
| A | LYS258 |
| A | IPE900 |
| A | MG907 |
| A | MG908 |
| A | MG909 |
| A | HOH918 |
| A | HOH922 |
| A | HOH933 |
| A | HOH945 |
| A | HOH1031 |
| A | HOH1032 |
| A | HOH1033 |
| A | HOH1034 |
| site_id | AC9 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE IPE B 902 |
| Chain | Residue |
| B | GLY65 |
| B | LYS66 |
| B | ARG69 |
| B | HIS98 |
| B | ARG117 |
| B | THR203 |
| B | PHE240 |
| B | GLN241 |
| B | RIS903 |
| B | HOH909 |
| B | HOH910 |
| B | HOH911 |
| B | HOH916 |
| B | HOH918 |
| B | HOH960 |
| site_id | BC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE RIS B 903 |
| Chain | Residue |
| B | MG906 |
| B | HOH913 |
| B | HOH927 |
| B | HOH933 |
| B | HOH945 |
| B | HOH983 |
| B | HOH999 |
| B | HOH1000 |
| B | HOH1001 |
| B | HOH1002 |
| B | ASP105 |
| B | ASP111 |
| B | ARG116 |
| B | GLN179 |
| B | LYS202 |
| B | THR203 |
| B | ASP244 |
| B | LYS258 |
| B | IPE902 |
| B | MG904 |
| B | MG905 |
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 | ASP111 | |
| A | ARG117 | |
| B | LYS66 | |
| B | ARG69 | |
| B | HIS98 | |
| B | ASP105 | |
| B | ASP111 | |
| B | ARG117 | |
| A | LYS66 | |
| A | ARG69 | |
| A | HIS98 | |
| A | ASP105 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: |
| Chain | Residue | Details |
| B | GLN241 | |
| B | LYS258 | |
| A | ARG116 | |
| A | LYS202 | |
| A | THR203 | |
| A | GLN241 | |
| A | LYS258 | |
| B | ARG116 | |
| B | LYS202 | |
| B | THR203 |
