5F05
Crystal structure of glutathione transferase F5 from Populus trichocarpa
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004364 | molecular_function | glutathione transferase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006749 | biological_process | glutathione metabolic process |
A | 0009407 | biological_process | toxin catabolic process |
A | 0016740 | molecular_function | transferase activity |
A | 0043295 | molecular_function | glutathione binding |
A | 0046872 | molecular_function | metal ion binding |
B | 0004364 | molecular_function | glutathione transferase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006749 | biological_process | glutathione metabolic process |
B | 0009407 | biological_process | toxin catabolic process |
B | 0016740 | molecular_function | transferase activity |
B | 0043295 | molecular_function | glutathione binding |
B | 0046872 | molecular_function | metal ion binding |
C | 0004364 | molecular_function | glutathione transferase activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0006749 | biological_process | glutathione metabolic process |
C | 0009407 | biological_process | toxin catabolic process |
C | 0016740 | molecular_function | transferase activity |
C | 0043295 | molecular_function | glutathione binding |
C | 0046872 | molecular_function | metal ion binding |
D | 0004364 | molecular_function | glutathione transferase activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0006749 | biological_process | glutathione metabolic process |
D | 0009407 | biological_process | toxin catabolic process |
D | 0016740 | molecular_function | transferase activity |
D | 0043295 | molecular_function | glutathione binding |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | binding site for residue GSH A 301 |
Chain | Residue |
A | SER12 |
A | HOH416 |
A | HOH427 |
A | HOH470 |
A | ASN14 |
A | HIS41 |
A | LYS42 |
A | GLN54 |
A | VAL55 |
A | GLU67 |
A | SER68 |
A | ARG69 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue GOL A 302 |
Chain | Residue |
A | LYS182 |
A | PHE185 |
A | ASP186 |
A | SER192 |
A | VAL195 |
A | HOH408 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue MG A 303 |
Chain | Residue |
A | HIS190 |
A | HOH443 |
A | HOH555 |
A | HOH564 |
site_id | AC4 |
Number of Residues | 15 |
Details | binding site for residue 12P B 301 |
Chain | Residue |
A | GLN73 |
A | ALA76 |
A | HIS77 |
A | GLY87 |
A | ALA88 |
A | LEU97 |
A | HOH574 |
B | GLN73 |
B | ALA76 |
B | HIS77 |
B | GLY87 |
B | ALA88 |
B | LEU97 |
B | GLN100 |
B | HOH551 |
site_id | AC5 |
Number of Residues | 18 |
Details | binding site for residue GSH B 302 |
Chain | Residue |
B | SER12 |
B | THR13 |
B | ASN14 |
B | HIS41 |
B | LYS42 |
B | GLY53 |
B | GLN54 |
B | VAL55 |
B | PRO56 |
B | GLU67 |
B | SER68 |
B | ARG69 |
B | HOH404 |
B | HOH428 |
B | HOH469 |
B | HOH492 |
B | HOH503 |
B | HOH552 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue PG4 B 303 |
Chain | Residue |
A | ASN91 |
B | ASP60 |
B | GLY61 |
B | ASP62 |
B | GLN78 |
B | HOH538 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue GOL B 304 |
Chain | Residue |
B | LYS182 |
B | ASP186 |
B | SER192 |
B | ALA196 |
B | HOH436 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue MG B 305 |
Chain | Residue |
B | HIS190 |
B | HOH439 |
B | HOH549 |
site_id | AC9 |
Number of Residues | 15 |
Details | binding site for residue GSH C 301 |
Chain | Residue |
C | SER12 |
C | ASN14 |
C | HIS41 |
C | LYS42 |
C | GLN54 |
C | VAL55 |
C | GLU67 |
C | SER68 |
C | ARG69 |
C | HOH404 |
C | HOH447 |
C | HOH502 |
C | HOH519 |
C | HOH552 |
D | HIS105 |
site_id | AD1 |
Number of Residues | 7 |
Details | binding site for residue GOL C 302 |
Chain | Residue |
C | LYS182 |
C | PHE185 |
C | ASP186 |
C | SER192 |
C | ALA196 |
C | HOH434 |
D | GOL304 |
site_id | AD2 |
Number of Residues | 14 |
Details | binding site for residue 12P D 301 |
Chain | Residue |
D | ALA76 |
D | HIS77 |
D | GLN85 |
D | LEU97 |
D | GLN100 |
D | HOH553 |
C | GLN73 |
C | ALA76 |
C | HIS77 |
C | GLY87 |
C | ALA88 |
C | LEU97 |
C | GLN100 |
C | HOH563 |
site_id | AD3 |
Number of Residues | 15 |
Details | binding site for residue GSH D 302 |
Chain | Residue |
C | HIS105 |
D | SER12 |
D | ASN14 |
D | HIS41 |
D | LYS42 |
D | GLN54 |
D | VAL55 |
D | GLU67 |
D | SER68 |
D | ARG69 |
D | HOH429 |
D | HOH469 |
D | HOH495 |
D | HOH502 |
D | HOH539 |
site_id | AD4 |
Number of Residues | 5 |
Details | binding site for residue PGE D 303 |
Chain | Residue |
C | ASN91 |
D | ASP60 |
D | ASP62 |
D | GLN78 |
D | HOH514 |
site_id | AD5 |
Number of Residues | 9 |
Details | binding site for residue GOL D 304 |
Chain | Residue |
C | GOL302 |
D | LYS182 |
D | PHE185 |
D | ASP186 |
D | SER192 |
D | VAL195 |
D | ALA196 |
D | HOH466 |
D | HOH533 |