3I4Z
Crystal structure of the dimethylallyl tryptophan synthase FgaPT2 from Aspergillus fumigatus
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 | 4 |
Details | BINDING SITE FOR RESIDUE BU2 A 460 |
Chain | Residue |
A | TYR191 |
A | ARG244 |
A | HOH505 |
A | HOH705 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE BU2 B 460 |
Chain | Residue |
B | ARG244 |
B | LEU263 |
B | TYR310 |
B | HOH547 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE BU2 A 461 |
Chain | Residue |
A | LEU81 |
A | LEU325 |
A | ALA397 |
A | BU2465 |
A | HOH553 |
A | HOH556 |
A | HOH628 |
A | ILE80 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE BU2 A 462 |
Chain | Residue |
A | LEU92 |
A | MET372 |
A | THR375 |
A | TYR376 |
A | THR379 |
A | TYR383 |
A | HOH712 |
A | HOH796 |
site_id | AC5 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE BU2 A 463 |
Chain | Residue |
A | ALA312 |
A | LEU315 |
A | ILE320 |
A | ASP322 |
A | GLU323 |
A | HOH528 |
B | TYR314 |
B | PRO316 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE BU2 B 461 |
Chain | Residue |
B | ILE80 |
B | LEU81 |
B | LEU325 |
B | ALA397 |
B | HOH491 |
B | HOH501 |
B | HOH554 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE BU2 A 464 |
Chain | Residue |
A | TYR84 |
A | LEU317 |
A | GLY318 |
A | TYR394 |
A | GLN415 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE BU2 A 465 |
Chain | Residue |
A | PRO326 |
A | TYR345 |
A | THR347 |
A | TYR398 |
A | BU2461 |
A | HOH815 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 466 |
Chain | Residue |
A | SER286 |
A | ARG404 |
A | ASP405 |
A | ARG406 |
A | HOH611 |
site_id | BC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 467 |
Chain | Residue |
A | THR119 |
A | HIS120 |
A | TRP123 |
A | LYS145 |
A | THR149 |
A | LEU150 |
A | ASP405 |
A | HOH611 |
A | HOH613 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 468 |
Chain | Residue |
A | ARG235 |
A | ALA271 |
A | ASP274 |
A | HOH493 |
A | HOH494 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 469 |
Chain | Residue |
A | LEU138 |
A | GLU139 |
A | ARG142 |
A | HOH489 |
A | HOH821 |
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 |