5LOL
Glutathione-bound Dehydroascorbate Reductase 2 of Arabidopsis thaliana
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004364 | molecular_function | glutathione transferase activity |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0009636 | biological_process | response to toxic substance |
| A | 0010731 | biological_process | protein glutathionylation |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019852 | biological_process | L-ascorbic acid metabolic process |
| A | 0033355 | biological_process | ascorbate glutathione cycle |
| A | 0043295 | molecular_function | glutathione binding |
| A | 0045174 | molecular_function | glutathione dehydrogenase (ascorbate) activity |
| A | 0080151 | biological_process | positive regulation of salicylic acid mediated signaling pathway |
| A | 0098869 | biological_process | cellular oxidant detoxification |
| A | 0140547 | biological_process | acquisition of seed longevity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue GSH A 301 |
| Chain | Residue |
| A | CYS20 |
| A | PHE22 |
| A | LYS47 |
| A | LYS59 |
| A | VAL60 |
| A | PRO61 |
| A | ASP72 |
| A | SER73 |
| A | HOH424 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 302 |
| Chain | Residue |
| A | LYS199 |
| A | LYS200 |
| A | GLU201 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 303 |
| Chain | Residue |
| A | LYS8 |
| A | LYS64 |
| A | TRP69 |
| A | LYS199 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 73 |
| Details | Domain: {"description":"GST N-terminal"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | Motif: {"description":"Glutathione-binding","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"Q65XA0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q65XA0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"28195196","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5LOL","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"S-glutathionyl cysteine","evidences":[{"source":"PubMed","id":"12077129","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
