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 | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
A | 1990229 | cellular_component | iron-sulfur cluster assembly complex |
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 | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
B | 1990229 | cellular_component | iron-sulfur cluster assembly complex |
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 | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:19505088 |
Chain | Residue | Details |
A | LYS22 | |
A | ARG59 | |
A | PHE71 | |
B | LYS22 | |
B | ARG59 | |
B | PHE71 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: |
Chain | Residue | Details |
A | CYS30 | |
A | CYS84 | |
B | CYS30 | |
B | CYS84 |