4JZB
Crystal Structure of Leshmaniasis major Farnesyl diphosphate synthase in complex with 1-(2-HYDROXY-2,2-DIPHOSPHONOETHYL)-3-PHENYLPYRIDINIUM, IPP and Ca2+
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 | 0008299 | biological_process | isoprenoid biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| 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 | (2E,6E)-farnesyl diphosphate synthase activity |
| B | 0004659 | molecular_function | prenyltransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008299 | biological_process | isoprenoid biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| 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 CA A 401 |
| Chain | Residue |
| A | ASP98 |
| A | ASP102 |
| A | CA402 |
| A | P2H405 |
| A | HOH502 |
| A | HOH503 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 402 |
| Chain | Residue |
| A | P2H405 |
| A | HOH501 |
| A | HOH504 |
| A | HOH511 |
| A | ASP98 |
| A | ASP102 |
| A | CA401 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 403 |
| Chain | Residue |
| A | ASP250 |
| A | P2H405 |
| A | HOH505 |
| A | HOH506 |
| A | HOH512 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE IPE A 404 |
| Chain | Residue |
| A | GLY47 |
| A | LYS48 |
| A | ARG51 |
| A | GLN91 |
| A | ARG108 |
| A | THR208 |
| A | TYR211 |
| A | PHE246 |
| A | GLN247 |
| A | ASP250 |
| A | P2H405 |
| A | HOH509 |
| A | HOH531 |
| A | HOH536 |
| A | HOH552 |
| A | HOH587 |
| A | HOH617 |
| A | HOH645 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE P2H A 405 |
| Chain | Residue |
| A | PHE94 |
| A | ASP98 |
| A | MET101 |
| A | ASP102 |
| A | ARG107 |
| A | THR163 |
| A | GLN167 |
| A | LYS207 |
| A | THR208 |
| A | ASP250 |
| A | LYS264 |
| A | CA401 |
| A | CA402 |
| A | CA403 |
| A | IPE404 |
| A | HOH504 |
| A | HOH513 |
| A | HOH532 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 406 |
| Chain | Residue |
| A | GLY266 |
| A | GLU270 |
| A | HOH554 |
| A | HOH561 |
| A | HOH671 |
| site_id | AC7 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE IPE B 401 |
| Chain | Residue |
| B | GLY47 |
| B | LYS48 |
| B | ARG51 |
| B | GLN91 |
| B | ARG108 |
| B | THR208 |
| B | TYR211 |
| B | PHE246 |
| B | GLN247 |
| B | ASP250 |
| B | P2H402 |
| B | HOH509 |
| B | HOH523 |
| B | HOH527 |
| B | HOH542 |
| B | HOH580 |
| B | HOH622 |
| B | HOH651 |
| site_id | AC8 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE P2H B 402 |
| Chain | Residue |
| B | PHE94 |
| B | ASP98 |
| B | MET101 |
| B | ASP102 |
| B | ARG107 |
| B | THR163 |
| B | GLN167 |
| B | LYS207 |
| B | THR208 |
| B | ASP250 |
| B | LYS264 |
| B | IPE401 |
| B | CA403 |
| B | CA404 |
| B | CA405 |
| B | HOH504 |
| B | HOH513 |
| B | HOH545 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 403 |
| Chain | Residue |
| B | HOH503 |
| B | HOH511 |
| B | ASP98 |
| B | ASP102 |
| B | P2H402 |
| B | CA405 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 404 |
| Chain | Residue |
| B | ASP250 |
| B | P2H402 |
| B | HOH505 |
| B | HOH506 |
| B | HOH514 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA B 405 |
| Chain | Residue |
| B | ASP98 |
| B | ASP102 |
| B | P2H402 |
| B | CA403 |
| B | HOH502 |
| B | HOH504 |
| B | HOH512 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 406 |
| Chain | Residue |
| B | GLY266 |
| B | GLU270 |
| B | HOH562 |
| B | HOH615 |
| B | HOH766 |
Functional Information from PROSITE/UniProt
