1ML6
Crystal Structure of mGSTA2-2 in Complex with the Glutathione Conjugate of Benzo[a]pyrene-7(R),8(S)-Diol-9(S),10(R)-Epoxide
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004364 | molecular_function | glutathione transferase activity |
A | 0005829 | cellular_component | cytosol |
A | 0006749 | biological_process | glutathione metabolic process |
A | 0006805 | biological_process | xenobiotic metabolic process |
A | 0009617 | biological_process | response to bacterium |
A | 0016740 | molecular_function | transferase activity |
A | 0035634 | biological_process | response to stilbenoid |
A | 0035731 | molecular_function | dinitrosyl-iron complex binding |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0043295 | molecular_function | glutathione binding |
B | 0004364 | molecular_function | glutathione transferase activity |
B | 0005829 | cellular_component | cytosol |
B | 0006749 | biological_process | glutathione metabolic process |
B | 0006805 | biological_process | xenobiotic metabolic process |
B | 0009617 | biological_process | response to bacterium |
B | 0016740 | molecular_function | transferase activity |
B | 0035634 | biological_process | response to stilbenoid |
B | 0035731 | molecular_function | dinitrosyl-iron complex binding |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0043295 | molecular_function | glutathione binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE GBX A 230 |
Chain | Residue |
A | TYR8 |
A | LEU207 |
A | ALA215 |
A | PHE221 |
A | HOH695 |
A | HOH845 |
B | ASP400 |
B | ARG430 |
B | HOH651 |
A | PHE9 |
A | LYS44 |
A | ASP52 |
A | GLN53 |
A | VAL54 |
A | GLN66 |
A | THR67 |
A | LEU110 |
site_id | AC2 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE GBX B 530 |
Chain | Residue |
A | ASP100 |
A | ARG130 |
A | HOH638 |
A | HOH852 |
B | PHE309 |
B | LYS344 |
B | GLN353 |
B | VAL354 |
B | PRO355 |
B | GLN366 |
B | THR367 |
B | LEU507 |
B | ILE512 |
B | ALA515 |
B | ARG516 |
B | PHE521 |
B | HOH681 |
B | HOH823 |
B | HOH833 |
B | HOH844 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IPA A 235 |
Chain | Residue |
A | ASP84 |
A | MET85 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IPA B 236 |
Chain | Residue |
B | THR376 |
B | ASP379 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P13745 |
Chain | Residue | Details |
A | PHE9 | |
B | PHE309 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000305|PubMed:12549910 |
Chain | Residue | Details |
A | LYS45 | |
A | VAL54 | |
A | THR67 | |
B | LYS345 | |
B | VAL354 | |
B | THR367 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P30115 |
Chain | Residue | Details |
A | GLY2 | |
B | GLY302 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P30115 |
Chain | Residue | Details |
A | PRO4 | |
B | PRO304 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1oe8 |
Chain | Residue | Details |
A | TYR8 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1oe8 |
Chain | Residue | Details |
B | TYR308 |