Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004659 | molecular_function | prenyltransferase activity |
A | 0008299 | biological_process | isoprenoid biosynthetic process |
A | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | binding site for residue SO4 A 401 |
Chain | Residue |
A | GLY47 |
A | HOH603 |
A | HOH612 |
A | LYS48 |
A | TYR49 |
A | PHE50 |
A | ARG51 |
A | GLN91 |
A | HOH547 |
A | HOH560 |
A | HOH580 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue SO4 A 402 |
Chain | Residue |
A | GLN21 |
A | HIS141 |
A | LYS158 |
A | HOH502 |
A | HOH527 |
A | HOH551 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue ACT A 403 |
Chain | Residue |
A | ASP191 |
A | ARG237 |
A | SER334 |
A | HOH538 |
A | HOH539 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue ZN A 404 |
Chain | Residue |
A | ASP98 |
A | ASP102 |
A | HOH501 |
A | HOH508 |
A | HOH553 |
A | HOH584 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue ZN A 405 |
Chain | Residue |
A | ASP250 |
A | HOH510 |
A | HOH543 |
A | HOH640 |
A | HOH685 |
site_id | AC6 |
Number of Residues | 11 |
Details | binding site for residue MJ4 A 406 |
Chain | Residue |
A | LEU95 |
A | ASP98 |
A | ARG107 |
A | GLN167 |
A | LYS207 |
A | TYR211 |
A | LYS264 |
A | HOH518 |
A | HOH571 |
A | HOH584 |
A | HOH640 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue SO4 A 407 |
Chain | Residue |
A | LYS48 |
A | PHE50 |
A | TYR213 |
A | PHE246 |
A | ARG360 |
Functional Information from PROSITE/UniProt
site_id | PS00444 |
Number of Residues | 13 |
Details | POLYPRENYL_SYNTHASE_2 Polyprenyl synthases signature 2. IGeyFQVqDDVmD |
Chain | Residue | Details |
A | ILE242-ASP254 | |
site_id | PS00723 |
Number of Residues | 15 |
Details | POLYPRENYL_SYNTHASE_1 Polyprenyl synthases signature 1. LVeDDim..DgsvmRRG |
Chain | Residue | Details |
A | LEU95-GLY109 | |