6B07
Crystal structure of CfFPPS2, a lepidopteran type-II farnesyl diphosphate synthase, complexed with [1-phosphono-2-(1-propylpyridin-2-yl)ethyl]phosphonic acid (inhibitor 1d)
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 |
B | 0004659 | molecular_function | prenyltransferase activity |
B | 0008299 | biological_process | isoprenoid biosynthetic process |
B | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
C | 0004659 | molecular_function | prenyltransferase activity |
C | 0008299 | biological_process | isoprenoid biosynthetic process |
C | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 24 |
Details | binding site for residue C6M A 401 |
Chain | Residue |
A | ARG104 |
A | GLN284 |
A | ASP287 |
A | LYS301 |
A | MG402 |
A | MG403 |
A | MG404 |
A | HOH528 |
A | HOH545 |
A | HOH559 |
A | HOH564 |
A | ASP147 |
A | HOH567 |
A | HOH571 |
A | HOH579 |
A | HOH645 |
A | HOH680 |
A | ASP151 |
A | ARG156 |
A | GLN215 |
A | LYS244 |
A | THR245 |
A | TYR248 |
A | PHE283 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue MG A 402 |
Chain | Residue |
A | ASP147 |
A | ASP151 |
A | C6M401 |
A | MG403 |
A | HOH536 |
A | HOH545 |
A | HOH703 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue MG A 403 |
Chain | Residue |
A | ASP147 |
A | ASP151 |
A | C6M401 |
A | MG402 |
A | HOH528 |
A | HOH680 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue MG A 404 |
Chain | Residue |
A | ASP287 |
A | C6M401 |
A | HOH559 |
A | HOH564 |
A | HOH645 |
site_id | AC5 |
Number of Residues | 4 |
Details | binding site for residue EDO A 405 |
Chain | Residue |
A | GLU84 |
A | HOH538 |
B | ARG236 |
B | HOH654 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue EDO A 406 |
Chain | Residue |
A | MET317 |
A | GLN320 |
A | HOH501 |
A | HOH628 |
B | GLN320 |
B | ARG321 |
site_id | AC7 |
Number of Residues | 25 |
Details | binding site for residue C6M B 401 |
Chain | Residue |
B | ARG104 |
B | ASP147 |
B | ASP151 |
B | ARG156 |
B | GLN215 |
B | LYS244 |
B | THR245 |
B | TYR248 |
B | PHE283 |
B | GLN284 |
B | ASP287 |
B | LYS301 |
B | MG402 |
B | MG403 |
B | MG404 |
B | HOH525 |
B | HOH534 |
B | HOH544 |
B | HOH568 |
B | HOH595 |
B | HOH598 |
B | HOH609 |
B | HOH617 |
B | HOH653 |
B | HOH710 |
site_id | AC8 |
Number of Residues | 7 |
Details | binding site for residue MG B 402 |
Chain | Residue |
B | ASP147 |
B | ASP151 |
B | C6M401 |
B | MG403 |
B | HOH534 |
B | HOH596 |
B | HOH710 |
site_id | AC9 |
Number of Residues | 6 |
Details | binding site for residue MG B 403 |
Chain | Residue |
B | ASP147 |
B | ASP151 |
B | C6M401 |
B | MG402 |
B | HOH525 |
B | HOH653 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue MG B 404 |
Chain | Residue |
B | ASP287 |
B | C6M401 |
B | HOH568 |
B | HOH609 |
B | HOH617 |
site_id | AD2 |
Number of Residues | 3 |
Details | binding site for residue EDO B 405 |
Chain | Residue |
B | PRO377 |
B | SER378 |
B | GLU379 |
site_id | AD3 |
Number of Residues | 4 |
Details | binding site for residue EDO B 406 |
Chain | Residue |
A | HOH723 |
B | GLU84 |
B | HOH538 |
A | ARG236 |
site_id | AD4 |
Number of Residues | 24 |
Details | binding site for residue C6M C 401 |
Chain | Residue |
C | ASP147 |
C | ASP151 |
C | ARG156 |
C | GLN215 |
C | LYS244 |
C | THR245 |
C | TYR248 |
C | PHE283 |
C | GLN284 |
C | ASP287 |
C | LYS301 |
C | MG402 |
C | MG403 |
C | MG404 |
C | HOH518 |
C | HOH534 |
C | HOH539 |
C | HOH556 |
C | HOH571 |
C | HOH572 |
C | HOH592 |
C | HOH648 |
C | HOH657 |
C | HOH663 |
site_id | AD5 |
Number of Residues | 7 |
Details | binding site for residue MG C 402 |
Chain | Residue |
C | ASP147 |
C | ASP151 |
C | C6M401 |
C | MG403 |
C | HOH518 |
C | HOH568 |
C | HOH663 |
site_id | AD6 |
Number of Residues | 6 |
Details | binding site for residue MG C 403 |
Chain | Residue |
C | ASP147 |
C | ASP151 |
C | C6M401 |
C | MG402 |
C | HOH534 |
C | HOH657 |
site_id | AD7 |
Number of Residues | 5 |
Details | binding site for residue MG C 404 |
Chain | Residue |
C | ASP287 |
C | C6M401 |
C | HOH571 |
C | HOH572 |
C | HOH592 |
site_id | AD8 |
Number of Residues | 7 |
Details | binding site for residue EDO C 405 |
Chain | Residue |
C | TYR95 |
C | ASN96 |
C | ASP148 |
C | CYS161 |
C | TRP162 |
C | HOH523 |
C | HOH564 |
site_id | AD9 |
Number of Residues | 2 |
Details | binding site for residue EDO C 406 |
Chain | Residue |
C | GLU84 |
C | HOH632 |
site_id | AE1 |
Number of Residues | 4 |
Details | binding site for residue EDO C 407 |
Chain | Residue |
C | PHE184 |
C | ASN205 |
C | GLU206 |
C | HOH629 |
Functional Information from PROSITE/UniProt