3WYW
Structural characterization of catalytic site of a Nilaparvata lugens delta-class glutathione transferase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004364 | molecular_function | glutathione transferase activity |
A | 0006749 | biological_process | glutathione metabolic process |
A | 0016740 | molecular_function | transferase activity |
B | 0003824 | molecular_function | catalytic activity |
B | 0004364 | molecular_function | glutathione transferase activity |
B | 0006749 | biological_process | glutathione metabolic process |
B | 0016740 | molecular_function | transferase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE GSH A 301 |
Chain | Residue |
A | SER11 |
A | SER67 |
A | ARG68 |
A | MET103 |
A | HOH402 |
A | HOH428 |
A | HOH430 |
A | HOH482 |
A | HOH510 |
A | HOH513 |
A | HOH555 |
A | PRO13 |
A | LEU35 |
A | GLN51 |
A | HIS52 |
A | ASN53 |
A | VAL54 |
A | PRO55 |
A | GLU66 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 302 |
Chain | Residue |
A | LYS94 |
A | GLN97 |
A | HOH470 |
B | LEU48 |
B | VAL63 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO A 303 |
Chain | Residue |
A | TYR6 |
A | PHE45 |
site_id | AC4 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE GSH B 301 |
Chain | Residue |
B | SER11 |
B | HIS52 |
B | ASN53 |
B | VAL54 |
B | PRO55 |
B | GLU66 |
B | SER67 |
B | ARG68 |
B | MET103 |
B | HOH406 |
B | HOH413 |
B | HOH427 |
B | HOH439 |
B | HOH465 |
B | HOH471 |
B | HOH474 |
B | HOH503 |
site_id | AC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO B 302 |
Chain | Residue |
B | TYR6 |
B | LEU48 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO B 303 |
Chain | Residue |
B | PRO2 |
B | ASP4 |
B | ASP58 |
B | ASN60 |
B | HOH573 |