4LLT
Crystal structure of a farnesyl diphosphate synthase from Roseobacter denitrificans OCh 114, target EFI-509393, with two IPP and calcium bound in active site
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004311 | molecular_function | geranylgeranyl diphosphate synthase activity |
| A | 0004659 | molecular_function | prenyltransferase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008299 | biological_process | isoprenoid biosynthetic process |
| A | 0015979 | biological_process | photosynthesis |
| A | 0015995 | biological_process | chlorophyll biosynthetic process |
| A | 0016114 | biological_process | terpenoid biosynthetic process |
| A | 0016117 | biological_process | carotenoid biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004311 | molecular_function | geranylgeranyl diphosphate synthase activity |
| B | 0004659 | molecular_function | prenyltransferase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008299 | biological_process | isoprenoid biosynthetic process |
| B | 0015979 | biological_process | photosynthesis |
| B | 0015995 | biological_process | chlorophyll biosynthetic process |
| B | 0016114 | biological_process | terpenoid biosynthetic process |
| B | 0016117 | biological_process | carotenoid biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE IPE A 301 |
| Chain | Residue |
| A | GLY40 |
| A | IPE302 |
| A | HOH404 |
| A | HOH409 |
| A | HOH410 |
| A | HOH423 |
| A | HOH424 |
| A | HOH436 |
| A | LYS41 |
| A | ARG44 |
| A | HIS73 |
| A | LEU77 |
| A | ARG92 |
| A | THR179 |
| A | PHE212 |
| A | ASP216 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE IPE A 302 |
| Chain | Residue |
| A | SER76 |
| A | ASP80 |
| A | ASP86 |
| A | ARG91 |
| A | MET149 |
| A | LYS178 |
| A | ASP216 |
| A | LYS230 |
| A | IPE301 |
| A | CA303 |
| A | CA304 |
| A | HOH457 |
| A | HOH464 |
| A | HOH537 |
| A | HOH538 |
| A | HOH540 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 303 |
| Chain | Residue |
| A | ASP216 |
| A | IPE302 |
| A | HOH458 |
| A | HOH472 |
| A | HOH489 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 304 |
| Chain | Residue |
| A | ASP80 |
| A | ASP86 |
| A | IPE302 |
| A | HOH462 |
| A | HOH538 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 305 |
| Chain | Residue |
| A | ASP86 |
| A | ASP156 |
| A | GLU160 |
| A | HOH457 |
| A | HOH464 |
| A | HOH527 |
| A | HOH528 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE IPE B 301 |
| Chain | Residue |
| B | GLY40 |
| B | LYS41 |
| B | ARG44 |
| B | HIS73 |
| B | LEU77 |
| B | ARG92 |
| B | THR179 |
| B | PHE212 |
| B | ASP216 |
| B | IPE302 |
| B | HOH410 |
| B | HOH420 |
| B | HOH430 |
| B | HOH439 |
| B | HOH446 |
| B | HOH456 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE IPE B 302 |
| Chain | Residue |
| B | LEU77 |
| B | ASP80 |
| B | ASP86 |
| B | ARG91 |
| B | LYS178 |
| B | ASP216 |
| B | LYS230 |
| B | IPE301 |
| B | CA303 |
| B | CA304 |
| B | HOH519 |
| B | HOH538 |
| B | HOH545 |
| B | HOH546 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 303 |
| Chain | Residue |
| B | ASP80 |
| B | ASP86 |
| B | IPE302 |
| B | HOH497 |
| B | HOH537 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 304 |
| Chain | Residue |
| B | ASP216 |
| B | IPE302 |
| B | HOH443 |
| B | HOH451 |
| B | HOH514 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 305 |
| Chain | Residue |
| B | ASP86 |
| B | ASP156 |
| B | HOH519 |
| B | HOH520 |
| B | HOH521 |
| B | HOH539 |
Functional Information from PROSITE/UniProt
