3I4X
Crystal structure of the dimethylallyl tryptophan synthase FgaPT2 from Aspergillus fumigatus in complex with Trp and DMSPP
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004659 | molecular_function | prenyltransferase activity |
A | 0009820 | biological_process | alkaloid metabolic process |
A | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
A | 0035835 | biological_process | indole alkaloid biosynthetic process |
A | 0035837 | biological_process | ergot alkaloid biosynthetic process |
A | 0050364 | molecular_function | tryptophan dimethylallyltransferase activity |
A | 1900809 | biological_process | fumigaclavine C biosynthetic process |
B | 0004659 | molecular_function | prenyltransferase activity |
B | 0009820 | biological_process | alkaloid metabolic process |
B | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
B | 0035835 | biological_process | indole alkaloid biosynthetic process |
B | 0035837 | biological_process | ergot alkaloid biosynthetic process |
B | 0050364 | molecular_function | tryptophan dimethylallyltransferase activity |
B | 1900809 | biological_process | fumigaclavine C biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE DST A 460 |
Chain | Residue |
A | ARG100 |
A | ARG404 |
A | TYR409 |
A | TYR413 |
A | TRP461 |
A | HOH588 |
A | HOH621 |
A | HOH627 |
A | HOH635 |
A | LYS187 |
A | TYR189 |
A | ARG257 |
A | LYS259 |
A | TYR261 |
A | MET328 |
A | GLN343 |
A | TYR345 |
site_id | AC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE TRP A 461 |
Chain | Residue |
A | ILE80 |
A | LEU81 |
A | GLU89 |
A | THR102 |
A | LYS174 |
A | TYR189 |
A | TYR191 |
A | ARG244 |
A | MET328 |
A | TYR398 |
A | DST460 |
A | HOH540 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 462 |
Chain | Residue |
A | VAL319 |
A | ILE320 |
A | ASP322 |
A | GLU323 |
A | HOH728 |
B | TYR314 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL A 463 |
Chain | Residue |
A | THR119 |
A | HIS120 |
A | TRP123 |
A | LYS145 |
A | THR149 |
A | LEU150 |
A | ASP405 |
A | HOH504 |
A | HOH572 |
A | HOH752 |
site_id | AC5 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE DST B 460 |
Chain | Residue |
B | ARG100 |
B | LYS187 |
B | TYR189 |
B | ARG257 |
B | LYS259 |
B | TYR261 |
B | MET328 |
B | GLN343 |
B | TYR345 |
B | ARG404 |
B | TYR409 |
B | TYR413 |
B | TRP461 |
B | HOH575 |
B | HOH680 |
B | HOH683 |
B | HOH720 |
site_id | AC6 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE TRP B 461 |
Chain | Residue |
B | ILE80 |
B | LEU81 |
B | GLU89 |
B | THR102 |
B | LYS174 |
B | TYR189 |
B | TYR191 |
B | ARG244 |
B | TYR398 |
B | DST460 |
B | HOH467 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 28 |
Details | BINDING: BINDING => ECO:0000269|PubMed:19706516 |
Chain | Residue | Details |
A | ILE80 | |
A | TYR261 | |
A | GLN343 | |
A | TYR345 | |
A | TYR409 | |
A | TYR413 | |
B | ILE80 | |
B | GLU89 | |
B | ARG100 | |
B | LYS187 | |
B | TYR189 | |
A | GLU89 | |
B | TYR191 | |
B | ARG244 | |
B | ARG257 | |
B | LYS259 | |
B | TYR261 | |
B | GLN343 | |
B | TYR345 | |
B | TYR409 | |
B | TYR413 | |
A | ARG100 | |
A | LYS187 | |
A | TYR189 | |
A | TYR191 | |
A | ARG244 | |
A | ARG257 | |
A | LYS259 |