4G0I
Glutathionyl-Hydroquinone Reductase, YqjG of Escherichia coli
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 | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 401 |
| Chain | Residue |
| A | VAL287 |
| A | ASN288 |
| A | PHE289 |
| A | ASP290 |
| A | HOH630 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 402 |
| Chain | Residue |
| A | ASP276 |
| A | HIS321 |
| A | SO4406 |
| A | HOH569 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 403 |
| Chain | Residue |
| A | TRP65 |
| A | ARG68 |
| A | TYR187 |
| A | ASN191 |
| A | HOH551 |
| A | HOH560 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 404 |
| Chain | Residue |
| A | TYR195 |
| A | HIS295 |
| A | HIS300 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 405 |
| Chain | Residue |
| A | PRO103 |
| A | GLY104 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 406 |
| Chain | Residue |
| A | ARG228 |
| A | ASP324 |
| A | SO4402 |
| A | HOH569 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MES A 407 |
| Chain | Residue |
| A | SER202 |
| A | GLN203 |
| A | GLU204 |
| B | ARG298 |
| B | THR306 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MES A 408 |
| Chain | Residue |
| A | GLY168 |
| A | ASP169 |
| A | TYR170 |
| A | ASN233 |
| A | GLN234 |
| A | LEU235 |
| A | HOH583 |
| B | LYS52 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 401 |
| Chain | Residue |
| B | VAL287 |
| B | ASN288 |
| B | PHE289 |
| B | ASP290 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 402 |
| Chain | Residue |
| B | ARG228 |
| B | ASP276 |
| B | HIS321 |
| B | SO4406 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 403 |
| Chain | Residue |
| B | TRP65 |
| B | ARG68 |
| B | TYR187 |
| B | ASN191 |
| B | ARG241 |
| B | HOH532 |
| B | HOH549 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 404 |
| Chain | Residue |
| B | MET91 |
| B | TYR195 |
| B | HIS295 |
| B | HIS300 |
| site_id | BC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 405 |
| Chain | Residue |
| B | PRO103 |
| B | GLY104 |
| site_id | BC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 406 |
| Chain | Residue |
| B | ARG228 |
| B | SO4402 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MES B 407 |
| Chain | Residue |
| B | ARG228 |
| B | ASN233 |
| B | GLN234 |
| B | LEU235 |
| B | HOH513 |
| B | HOH614 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 248 |
| Details | Domain: {"description":"GST C-terminal"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 216 |
| Details | Region: {"description":"Dimerization"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"22955277","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"22955277","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22955277","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2012","submissionDatabase":"PDB data bank","title":"Crystal structure analysis of YqjG from Escherichia coli.","authors":["Branch M.C.","Cook P.D.","Harp J.M.","Armstrong R.N."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Site: {"description":"Lowers pKa of active site Cys","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
