4G0K
Glutathionyl-hydroquinone reductase, YqjG, of E.coli complexed with GS-menadione
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004364 | molecular_function | glutathione transferase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016672 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor |
A | 0042803 | molecular_function | protein homodimerization activity |
B | 0004364 | molecular_function | glutathione transferase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016672 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor |
B | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 401 |
Chain | Residue |
A | ARG73 |
A | LYS74 |
A | GLU285 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 402 |
Chain | Residue |
A | ASP276 |
A | GLN279 |
A | HIS321 |
A | SO4406 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 403 |
Chain | Residue |
A | LYS261 |
A | HIS262 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 404 |
Chain | Residue |
A | HIS262 |
A | ASP266 |
A | HOH560 |
A | HOH577 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 405 |
Chain | Residue |
A | PRO103 |
A | GLY104 |
A | HOH537 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 406 |
Chain | Residue |
A | ARG228 |
A | ASP324 |
A | SO4402 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 407 |
Chain | Residue |
A | ASN288 |
A | PHE289 |
A | ASP290 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE MES A 408 |
Chain | Residue |
A | GLY168 |
A | ASP169 |
A | TYR170 |
A | TYR229 |
A | GLN234 |
A | LEU235 |
A | HOH542 |
B | LYS52 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MES A 409 |
Chain | Residue |
A | SER202 |
A | GLN203 |
A | GLU204 |
B | THR306 |
site_id | BC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE MES A 410 |
Chain | Residue |
A | TRP65 |
A | ARG68 |
A | GLU148 |
A | ALA150 |
A | GLY184 |
A | TYR187 |
A | ARG241 |
A | 0VS411 |
site_id | BC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE 0VS A 411 |
Chain | Residue |
A | CYS63 |
A | TRP65 |
A | TRP96 |
A | ARG130 |
A | THR132 |
A | VAL133 |
A | PRO134 |
A | ASN147 |
A | GLU148 |
A | SER149 |
A | MES410 |
site_id | BC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE SO4 B 401 |
Chain | Residue |
B | ARG73 |
site_id | BC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 B 402 |
Chain | Residue |
B | TRP65 |
B | ARG68 |
B | GLU148 |
B | ALA150 |
B | TYR187 |
B | ARG241 |
B | 0VS410 |
site_id | BC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 B 403 |
Chain | Residue |
B | LYS261 |
B | HIS262 |
site_id | BC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 B 404 |
Chain | Residue |
B | PRO103 |
B | GLY104 |
site_id | BC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 405 |
Chain | Residue |
B | VAL287 |
B | ASN288 |
B | PHE289 |
B | ASP290 |
site_id | BC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 406 |
Chain | Residue |
B | HIS262 |
B | ASP266 |
B | HOH549 |
site_id | BC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 407 |
Chain | Residue |
B | ARG228 |
B | ASP324 |
B | MES409 |
site_id | CC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 408 |
Chain | Residue |
B | SER202 |
B | GLN203 |
B | GLU204 |
site_id | CC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MES B 409 |
Chain | Residue |
B | ASP169 |
B | TYR170 |
B | TYR229 |
B | GLN234 |
B | LEU235 |
B | SO4407 |
site_id | CC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE 0VS B 410 |
Chain | Residue |
B | TRP65 |
B | TRP96 |
B | ARG130 |
B | THR132 |
B | VAL133 |
B | PRO134 |
B | ASN147 |
B | GLU148 |
B | SER149 |
B | SO4402 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:22955277 |
Chain | Residue | Details |
A | CYS63 | |
B | CYS63 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:22955277 |
Chain | Residue | Details |
A | TYR195 | |
B | TYR195 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22955277, ECO:0000269|Ref.5 |
Chain | Residue | Details |
A | TRP96 | |
A | ARG130 | |
A | GLU148 | |
B | TRP96 | |
B | ARG130 | |
B | GLU148 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | SITE: Lowers pKa of active site Cys => ECO:0000305 |
Chain | Residue | Details |
A | TYR253 | |
A | TYR296 | |
B | TYR253 | |
B | TYR296 |