2WCI
Structure of E. coli monothiol glutaredoxin GRX4 homodimer
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006879 | biological_process | intracellular iron ion homeostasis |
| A | 0015036 | molecular_function | disulfide oxidoreductase activity |
| A | 0016226 | biological_process | iron-sulfur cluster assembly |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0045454 | biological_process | cell redox homeostasis |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006879 | biological_process | intracellular iron ion homeostasis |
| B | 0015036 | molecular_function | disulfide oxidoreductase activity |
| B | 0016226 | biological_process | iron-sulfur cluster assembly |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0045454 | biological_process | cell redox homeostasis |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FES A 1114 |
| Chain | Residue |
| A | LYS22 |
| A | CYS30 |
| A | GSH1115 |
| B | LYS22 |
| B | CYS30 |
| B | GSH1115 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE GSH A 1115 |
| Chain | Residue |
| A | ARG59 |
| A | THR70 |
| A | PHE71 |
| A | GLY83 |
| A | CYS84 |
| A | ASP85 |
| A | FES1114 |
| A | HOH2075 |
| A | HOH2089 |
| A | HOH2090 |
| A | HOH2092 |
| A | HOH2094 |
| A | HOH2096 |
| A | HOH2097 |
| B | ASP85 |
| B | HOH2027 |
| A | LYS22 |
| A | CYS30 |
| A | PHE32 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 1116 |
| Chain | Residue |
| A | PRO28 |
| A | CYS30 |
| A | GLY31 |
| A | HOH2009 |
| A | HOH2012 |
| B | ARG59 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE GSH B 1115 |
| Chain | Residue |
| A | THR70 |
| A | FES1114 |
| A | HOH2094 |
| B | LYS22 |
| B | CYS30 |
| B | PHE32 |
| B | ARG59 |
| B | THR70 |
| B | PHE71 |
| B | GLY83 |
| B | CYS84 |
| B | ASP85 |
| B | HOH2062 |
| B | HOH2066 |
| B | HOH2081 |
| B | HOH2082 |
| B | HOH2083 |
| B | HOH2084 |
| B | HOH2085 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 204 |
| Details | Domain: {"description":"Glutaredoxin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00686","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"19505088","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {} |
| Chain | Residue | Details |
