1GUM
HUMAN GLUTATHIONE TRANSFERASE A4-4 WITHOUT LIGANDS
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004364 | molecular_function | glutathione transferase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006749 | biological_process | glutathione metabolic process |
A | 0006805 | biological_process | xenobiotic metabolic process |
A | 0016740 | molecular_function | transferase activity |
A | 0042802 | molecular_function | identical protein binding |
A | 0042803 | molecular_function | protein homodimerization activity |
B | 0004364 | molecular_function | glutathione transferase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006749 | biological_process | glutathione metabolic process |
B | 0006805 | biological_process | xenobiotic metabolic process |
B | 0016740 | molecular_function | transferase activity |
B | 0042802 | molecular_function | identical protein binding |
B | 0042803 | molecular_function | protein homodimerization activity |
C | 0004364 | molecular_function | glutathione transferase activity |
C | 0005515 | molecular_function | protein binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0006749 | biological_process | glutathione metabolic process |
C | 0006805 | biological_process | xenobiotic metabolic process |
C | 0016740 | molecular_function | transferase activity |
C | 0042802 | molecular_function | identical protein binding |
C | 0042803 | molecular_function | protein homodimerization activity |
D | 0004364 | molecular_function | glutathione transferase activity |
D | 0005515 | molecular_function | protein binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0006749 | biological_process | glutathione metabolic process |
D | 0006805 | biological_process | xenobiotic metabolic process |
D | 0016740 | molecular_function | transferase activity |
D | 0042802 | molecular_function | identical protein binding |
D | 0042803 | molecular_function | protein homodimerization activity |
E | 0004364 | molecular_function | glutathione transferase activity |
E | 0005515 | molecular_function | protein binding |
E | 0005737 | cellular_component | cytoplasm |
E | 0005829 | cellular_component | cytosol |
E | 0006749 | biological_process | glutathione metabolic process |
E | 0006805 | biological_process | xenobiotic metabolic process |
E | 0016740 | molecular_function | transferase activity |
E | 0042802 | molecular_function | identical protein binding |
E | 0042803 | molecular_function | protein homodimerization activity |
F | 0004364 | molecular_function | glutathione transferase activity |
F | 0005515 | molecular_function | protein binding |
F | 0005737 | cellular_component | cytoplasm |
F | 0005829 | cellular_component | cytosol |
F | 0006749 | biological_process | glutathione metabolic process |
F | 0006805 | biological_process | xenobiotic metabolic process |
F | 0016740 | molecular_function | transferase activity |
F | 0042802 | molecular_function | identical protein binding |
F | 0042803 | molecular_function | protein homodimerization activity |
G | 0004364 | molecular_function | glutathione transferase activity |
G | 0005515 | molecular_function | protein binding |
G | 0005737 | cellular_component | cytoplasm |
G | 0005829 | cellular_component | cytosol |
G | 0006749 | biological_process | glutathione metabolic process |
G | 0006805 | biological_process | xenobiotic metabolic process |
G | 0016740 | molecular_function | transferase activity |
G | 0042802 | molecular_function | identical protein binding |
G | 0042803 | molecular_function | protein homodimerization activity |
H | 0004364 | molecular_function | glutathione transferase activity |
H | 0005515 | molecular_function | protein binding |
H | 0005737 | cellular_component | cytoplasm |
H | 0005829 | cellular_component | cytosol |
H | 0006749 | biological_process | glutathione metabolic process |
H | 0006805 | biological_process | xenobiotic metabolic process |
H | 0016740 | molecular_function | transferase activity |
H | 0042802 | molecular_function | identical protein binding |
H | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
site_id | GTA |
Number of Residues | 11 |
Details | GLUTATHIONE BINDING SITE. |
Chain | Residue |
A | TYR9 |
A | ARG131 |
A | PHE220 |
A | ARG15 |
A | LEU41 |
A | GLN45 |
A | GLN54 |
A | VAL55 |
A | GLN67 |
A | THR68 |
A | ASP101 |
site_id | GTB |
Number of Residues | 11 |
Details | GLUTATHIONE BINDING SITE. |
Chain | Residue |
B | TYR9 |
B | ARG15 |
B | LEU41 |
B | GLN45 |
B | GLN54 |
B | VAL55 |
B | GLN67 |
B | THR68 |
B | ASP101 |
B | ARG131 |
B | PHE220 |
site_id | GTC |
Number of Residues | 11 |
Details | GLUTATHIONE BINDING SITE. |
Chain | Residue |
C | TYR9 |
C | ARG15 |
C | LEU41 |
C | GLN45 |
C | GLN54 |
C | VAL55 |
C | GLN67 |
C | THR68 |
C | ASP101 |
C | ARG131 |
C | PHE220 |
site_id | GTD |
Number of Residues | 11 |
Details | GLUTATHIONE BINDING SITE. |
Chain | Residue |
D | TYR9 |
D | ARG15 |
D | LEU41 |
D | GLN45 |
D | GLN54 |
D | VAL55 |
D | GLN67 |
D | THR68 |
D | ASP101 |
D | ARG131 |
D | PHE220 |
site_id | GTE |
Number of Residues | 11 |
Details | GLUTATHIONE BINDING SITE. |
Chain | Residue |
E | TYR9 |
E | ARG15 |
E | LEU41 |
E | GLN45 |
E | GLN54 |
E | VAL55 |
E | GLN67 |
E | THR68 |
E | ASP101 |
E | ARG131 |
E | PHE220 |
site_id | GTF |
Number of Residues | 1 |
Details | GLUTATHIONE BINDING SITE. |
Chain | Residue |
F | TYR9 |
site_id | GTG |
Number of Residues | 11 |
Details | GLUTATHIONE BINDING SITE. |
Chain | Residue |
G | LEU41 |
G | GLN45 |
G | GLN54 |
G | VAL55 |
G | GLN67 |
G | THR68 |
G | ASP101 |
G | ARG131 |
G | PHE220 |
G | TYR9 |
G | ARG15 |
site_id | GTH |
Number of Residues | 11 |
Details | GLUTATHIONE BINDING SITE. |
Chain | Residue |
H | TYR9 |
H | ARG15 |
H | LEU41 |
H | GLN45 |
H | GLN54 |
H | VAL55 |
H | GLN67 |
H | THR68 |
H | ASP101 |
H | ARG131 |
H | PHE220 |
site_id | HTA |
Number of Residues | 8 |
Details | ELECTROPHILIC SUBSTRATE BINDING SITE. |
Chain | Residue |
A | GLY14 |
A | GLU104 |
A | ILE107 |
A | MET108 |
A | PHE111 |
A | TYR212 |
A | VAL216 |
A | TYR217 |
site_id | HTB |
Number of Residues | 8 |
Details | ELECTROPHILIC SUBSTRATE BINDING SITE. |
Chain | Residue |
B | GLY14 |
B | GLU104 |
B | ILE107 |
B | MET108 |
B | PHE111 |
B | TYR212 |
B | VAL216 |
B | TYR217 |
site_id | HTC |
Number of Residues | 8 |
Details | ELECTROPHILIC SUBSTRATE BINDING SITE. |
Chain | Residue |
C | GLY14 |
C | GLU104 |
C | ILE107 |
C | MET108 |
C | PHE111 |
C | TYR212 |
C | VAL216 |
C | TYR217 |
site_id | HTD |
Number of Residues | 8 |
Details | ELECTROPHILIC SUBSTRATE BINDING SITE. |
Chain | Residue |
D | GLY14 |
D | GLU104 |
D | ILE107 |
D | MET108 |
D | PHE111 |
D | TYR212 |
D | VAL216 |
D | TYR217 |
site_id | HTE |
Number of Residues | 8 |
Details | ELECTROPHILIC SUBSTRATE BINDING SITE. |
Chain | Residue |
E | GLY14 |
E | GLU104 |
E | ILE107 |
E | MET108 |
E | PHE111 |
E | TYR212 |
E | VAL216 |
E | TYR217 |
site_id | HTF |
Number of Residues | 1 |
Details | ELECTROPHILIC SUBSTRATE BINDING SITE. |
Chain | Residue |
F | GLY14 |
site_id | HTG |
Number of Residues | 8 |
Details | ELECTROPHILIC SUBSTRATE BINDING SITE. |
Chain | Residue |
G | GLY14 |
G | GLU104 |
G | ILE107 |
G | MET108 |
G | PHE111 |
G | TYR212 |
G | VAL216 |
G | TYR217 |
site_id | HTH |
Number of Residues | 8 |
Details | ELECTROPHILIC SUBSTRATE BINDING SITE. |
Chain | Residue |
H | GLY14 |
H | GLU104 |
H | ILE107 |
H | MET108 |
H | PHE111 |
H | TYR212 |
H | VAL216 |
H | TYR217 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P13745 |
Chain | Residue | Details |
A | TYR9 | |
E | GLN67 | |
F | TYR9 | |
F | GLN67 | |
G | TYR9 | |
G | GLN67 | |
H | TYR9 | |
H | GLN67 | |
A | GLN67 | |
B | TYR9 | |
B | GLN67 | |
C | TYR9 | |
C | GLN67 | |
D | TYR9 | |
D | GLN67 | |
E | TYR9 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P30711 |
Chain | Residue | Details |
A | GLN54 | |
B | GLN54 | |
C | GLN54 | |
D | GLN54 | |
E | GLN54 | |
F | GLN54 | |
G | GLN54 | |
H | GLN54 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000305 |
Chain | Residue | Details |
A | TYR212 | |
B | TYR212 | |
C | TYR212 | |
D | TYR212 | |
E | TYR212 | |
F | TYR212 | |
G | TYR212 | |
H | TYR212 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | MOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:P14942 |
Chain | Residue | Details |
A | MET1 | |
B | MET1 | |
C | MET1 | |
D | MET1 | |
E | MET1 | |
F | MET1 | |
G | MET1 | |
H | MET1 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1oe8 |
Chain | Residue | Details |
A | TYR9 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1oe8 |
Chain | Residue | Details |
B | TYR9 |
site_id | CSA3 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1oe8 |
Chain | Residue | Details |
C | TYR9 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1oe8 |
Chain | Residue | Details |
D | TYR9 |
site_id | CSA5 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1oe8 |
Chain | Residue | Details |
E | TYR9 |
site_id | CSA6 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1oe8 |
Chain | Residue | Details |
F | TYR9 |
site_id | CSA7 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1oe8 |
Chain | Residue | Details |
G | TYR9 |
site_id | CSA8 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1oe8 |
Chain | Residue | Details |
H | TYR9 |