2FOR
Crystal Structure of the Shigella flexneri Farnesyl Pyrophosphate Synthase Complex with an Isopentenyl Pyrophosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 0008654 | biological_process | phospholipid biosynthetic process |
| A | 0016114 | biological_process | terpenoid biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0045337 | biological_process | farnesyl diphosphate biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0120531 | molecular_function | prenyl diphosphate synthase 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 | 0008654 | biological_process | phospholipid biosynthetic process |
| B | 0016114 | biological_process | terpenoid biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0045337 | biological_process | farnesyl diphosphate biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0120531 | molecular_function | prenyl diphosphate synthase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 A 300 |
| Chain | Residue |
| A | GLY44 |
| A | LYS45 |
| A | HIS77 |
| A | ARG96 |
| A | PO4301 |
| A | HOH438 |
| A | HOH439 |
| A | HOH440 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A 301 |
| Chain | Residue |
| A | HIS77 |
| A | PO4300 |
| A | HOH442 |
| A | HOH443 |
| A | HOH454 |
| A | ARG48 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 302 |
| Chain | Residue |
| A | ASP161 |
| A | LYS181 |
| A | LYS247 |
| A | HOH444 |
| A | HOH445 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 B 300 |
| Chain | Residue |
| B | GLY44 |
| B | LYS45 |
| B | HIS77 |
| B | ARG96 |
| B | PO4301 |
| B | IPR302 |
| B | HOH463 |
| B | HOH465 |
| B | HOH468 |
| B | HOH469 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 B 301 |
| Chain | Residue |
| B | ARG48 |
| B | HIS77 |
| B | PO4300 |
| B | HOH453 |
| B | HOH467 |
| B | HOH468 |
| B | HOH481 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A 303 |
| Chain | Residue |
| A | ARG176 |
| A | ARG179 |
| A | HIS180 |
| A | PO4304 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PO4 A 304 |
| Chain | Residue |
| A | ARG187 |
| A | PO4303 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE IPR A 305 |
| Chain | Residue |
| A | LYS45 |
| A | LEU47 |
| A | ARG48 |
| A | ASP223 |
| A | ARG297 |
| A | HOH437 |
| A | HOH440 |
| A | HOH442 |
| A | HOH443 |
| A | HOH454 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE IPR B 302 |
| Chain | Residue |
| B | LYS45 |
| B | LEU47 |
| B | ARG48 |
| B | HIS77 |
| B | ARG95 |
| B | PO4300 |
| B | HOH456 |
| B | HOH465 |
| B | HOH467 |
| B | HOH468 |
| B | HOH481 |
Functional Information from PROSITE/UniProt
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1fps |
| Chain | Residue | Details |
| A | ARG95 | |
| A | PHE219 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1fps |
| Chain | Residue | Details |
| B | ARG95 | |
| B | PHE219 |
